PubMed:6896661 JSONTXT

{"project":"Test-Species-PubTator","denotations":[{"id":"2","span":{"begin":15,"end":46},"obj":"Gene"},{"id":"3","span":{"begin":54,"end":67},"obj":"Chemical"},{"id":"33","span":{"begin":95,"end":137},"obj":"Gene"},{"id":"34","span":{"begin":139,"end":148},"obj":"Gene"},{"id":"35","span":{"begin":305,"end":314},"obj":"Gene"},{"id":"36","span":{"begin":364,"end":377},"obj":"Chemical"},{"id":"37","span":{"begin":392,"end":408},"obj":"Chemical"},{"id":"38","span":{"begin":444,"end":460},"obj":"Chemical"},{"id":"39","span":{"begin":464,"end":476},"obj":"Chemical"},{"id":"40","span":{"begin":477,"end":493},"obj":"Chemical"},{"id":"41","span":{"begin":582,"end":598},"obj":"Chemical"},{"id":"42","span":{"begin":629,"end":638},"obj":"Gene"},{"id":"43","span":{"begin":669,"end":672},"obj":"Chemical"},{"id":"44","span":{"begin":673,"end":687},"obj":"Chemical"},{"id":"45","span":{"begin":786,"end":796},"obj":"Gene"},{"id":"46","span":{"begin":844,"end":857},"obj":"Chemical"},{"id":"47","span":{"begin":862,"end":878},"obj":"Chemical"},{"id":"48","span":{"begin":917,"end":926},"obj":"Gene"},{"id":"49","span":{"begin":934,"end":947},"obj":"Chemical"},{"id":"50","span":{"begin":1093,"end":1102},"obj":"Gene"},{"id":"51","span":{"begin":1106,"end":1119},"obj":"Chemical"},{"id":"52","span":{"begin":1142,"end":1146},"obj":"Chemical"},{"id":"53","span":{"begin":1148,"end":1152},"obj":"Chemical"},{"id":"54","span":{"begin":1155,"end":1157},"obj":"Chemical"},{"id":"55","span":{"begin":1158,"end":1161},"obj":"Chemical"},{"id":"56","span":{"begin":1172,"end":1181},"obj":"Gene"},{"id":"57","span":{"begin":1276,"end":1285},"obj":"Gene"},{"id":"58","span":{"begin":1338,"end":1354},"obj":"Chemical"},{"id":"59","span":{"begin":1444,"end":1453},"obj":"Gene"},{"id":"60","span":{"begin":1461,"end":1474},"obj":"Chemical"},{"id":"61","span":{"begin":1636,"end":1650},"obj":"Gene"}],"attributes":[{"id":"A3","pred":"resolved_to","subj":"3","obj":"MESH:D011122"},{"id":"A36","pred":"resolved_to","subj":"36","obj":"MESH:C033190"},{"id":"A37","pred":"resolved_to","subj":"37","obj":"MESH:C008881"},{"id":"A38","pred":"resolved_to","subj":"38","obj":"-"},{"id":"A39","pred":"resolved_to","subj":"39","obj":"-"},{"id":"A40","pred":"resolved_to","subj":"40","obj":"-"},{"id":"A41","pred":"resolved_to","subj":"41","obj":"MESH:C008881"},{"id":"A43","pred":"resolved_to","subj":"43","obj":"MESH:D012967"},{"id":"A44","pred":"resolved_to","subj":"44","obj":"MESH:C016679"},{"id":"A46","pred":"resolved_to","subj":"46","obj":"MESH:C033190"},{"id":"A47","pred":"resolved_to","subj":"47","obj":"MESH:C008881"},{"id":"A49","pred":"resolved_to","subj":"49","obj":"MESH:D011122"},{"id":"A51","pred":"resolved_to","subj":"51","obj":"MESH:C033190"},{"id":"A52","pred":"resolved_to","subj":"52","obj":"-"},{"id":"A53","pred":"resolved_to","subj":"53","obj":"-"},{"id":"A54","pred":"resolved_to","subj":"54","obj":"MESH:D014316"},{"id":"A55","pred":"resolved_to","subj":"55","obj":"MESH:C000615311"},{"id":"A58","pred":"resolved_to","subj":"58","obj":"MESH:C008881"},{"id":"A60","pred":"resolved_to","subj":"60","obj":"MESH:D011122"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"Test-Species-PubDictionaries","denotations":[{"id":"T1","span":{"begin":15,"end":30},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":95,"end":110},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":112,"end":116},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":187,"end":191},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1635,"end":1639},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1891767"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1891767"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1891767"},{"id":"A5","pred":"db_id","subj":"T5","obj":"1891767"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"Test-Species-PubDictionaries-PubMedBERT","denotations":[{"id":"T1","span":{"begin":15,"end":30},"obj":"Species"},{"id":"T2","span":{"begin":95,"end":110},"obj":"Species"},{"id":"T3","span":{"begin":112,"end":116},"obj":"Species"},{"id":"T4","span":{"begin":187,"end":191},"obj":"Species"},{"id":"T5","span":{"begin":1635,"end":1639},"obj":"Species"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1891767"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1891767"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1891767"},{"id":"A5","pred":"db_id","subj":"T5","obj":"1891767"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"mondo_disease","denotations":[{"id":"T1","span":{"begin":124,"end":129},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MONDO_0005070"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-Glycan","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"Glycan"},{"id":"T2","span":{"begin":139,"end":148},"obj":"Glycan"},{"id":"T3","span":{"begin":305,"end":314},"obj":"Glycan"},{"id":"T4","span":{"begin":629,"end":638},"obj":"Glycan"},{"id":"T5","span":{"begin":917,"end":926},"obj":"Glycan"},{"id":"T6","span":{"begin":1093,"end":1102},"obj":"Glycan"},{"id":"T7","span":{"begin":1171,"end":1180},"obj":"Glycan"},{"id":"T8","span":{"begin":1275,"end":1284},"obj":"Glycan"},{"id":"T9","span":{"begin":1443,"end":1452},"obj":"Glycan"},{"id":"T10","span":{"begin":1640,"end":1649},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"Glycan-GlyCosmos","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"Glycan"},{"id":"T2","span":{"begin":139,"end":148},"obj":"Glycan"},{"id":"T3","span":{"begin":305,"end":314},"obj":"Glycan"},{"id":"T4","span":{"begin":629,"end":638},"obj":"Glycan"},{"id":"T5","span":{"begin":917,"end":926},"obj":"Glycan"},{"id":"T6","span":{"begin":1093,"end":1102},"obj":"Glycan"},{"id":"T7","span":{"begin":1171,"end":1180},"obj":"Glycan"},{"id":"T8","span":{"begin":1275,"end":1284},"obj":"Glycan"},{"id":"T9","span":{"begin":1443,"end":1452},"obj":"Glycan"},{"id":"T10","span":{"begin":1640,"end":1649},"obj":"Glycan"}],"attributes":[{"id":"A1","pred":"glycosmos_id","subj":"T1","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A11","pred":"image","subj":"T1","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A2","pred":"glycosmos_id","subj":"T2","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A12","pred":"image","subj":"T2","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A3","pred":"glycosmos_id","subj":"T3","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A13","pred":"image","subj":"T3","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A4","pred":"glycosmos_id","subj":"T4","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A14","pred":"image","subj":"T4","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A5","pred":"glycosmos_id","subj":"T5","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A15","pred":"image","subj":"T5","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A6","pred":"glycosmos_id","subj":"T6","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A16","pred":"image","subj":"T6","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A7","pred":"glycosmos_id","subj":"T7","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A17","pred":"image","subj":"T7","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A8","pred":"glycosmos_id","subj":"T8","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A18","pred":"image","subj":"T8","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A9","pred":"glycosmos_id","subj":"T9","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A19","pred":"image","subj":"T9","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"},{"id":"A10","pred":"glycosmos_id","subj":"T10","obj":"https://glycosmos.org/glycans/show/G00031MO"},{"id":"A20","pred":"image","subj":"T10","obj":"https://api.glycosmos.org/wurcs2image/latest/png/binary/G00031MO"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-HP","denotations":[{"id":"T1","span":{"begin":124,"end":129},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-MONDO","denotations":[{"id":"T1","span":{"begin":124,"end":129},"obj":"Disease"}],"attributes":[{"id":"A1","pred":"mondo_id","subj":"T1","obj":"MONDO:0005070"}],"namespaces":[{"prefix":"MONDO","uri":"http://purl.obolibrary.org/obo/MONDO_"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-Taxon","denotations":[{"id":"T1","span":{"begin":15,"end":30},"obj":"Organism"},{"id":"T2","span":{"begin":95,"end":110},"obj":"Organism"},{"id":"T3","span":{"begin":112,"end":116},"obj":"Organism"},{"id":"T4","span":{"begin":187,"end":191},"obj":"Organism"},{"id":"T5","span":{"begin":1635,"end":1639},"obj":"Organism"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1891767"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1891767"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1891767"},{"id":"A5","pred":"db_id","subj":"T5","obj":"1891767"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-Sentences","blocks":[{"id":"T1","span":{"begin":0,"end":94},"obj":"Sentence"},{"id":"T2","span":{"begin":95,"end":254},"obj":"Sentence"},{"id":"T3","span":{"begin":255,"end":423},"obj":"Sentence"},{"id":"T4","span":{"begin":424,"end":785},"obj":"Sentence"},{"id":"T5","span":{"begin":786,"end":879},"obj":"Sentence"},{"id":"T6","span":{"begin":880,"end":1017},"obj":"Sentence"},{"id":"T7","span":{"begin":1018,"end":1153},"obj":"Sentence"},{"id":"T8","span":{"begin":1154,"end":1354},"obj":"Sentence"},{"id":"T9","span":{"begin":1355,"end":1549},"obj":"Sentence"},{"id":"T10","span":{"begin":1550,"end":1707},"obj":"Sentence"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":139,"end":148},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":305,"end":314},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":629,"end":638},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":917,"end":926},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1093,"end":1102},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1171,"end":1180},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1275,"end":1284},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1443,"end":1452},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1640,"end":1649},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-UBERON","denotations":[{"id":"T1","span":{"begin":68,"end":76},"obj":"Body_part"},{"id":"T2","span":{"begin":948,"end":956},"obj":"Body_part"},{"id":"T3","span":{"begin":1474,"end":1482},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos15-FMA","denotations":[{"id":"T1","span":{"begin":68,"end":76},"obj":"Body_part"},{"id":"T2","span":{"begin":948,"end":956},"obj":"Body_part"},{"id":"T3","span":{"begin":1474,"end":1482},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"FMA:13478"},{"id":"A2","pred":"db_id","subj":"T2","obj":"FMA:13478"},{"id":"A3","pred":"db_id","subj":"T3","obj":"FMA:13478"}],"namespaces":[{"prefix":"FMA","uri":"http://purl.org/sig/ont/fma/fma"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":15,"end":30},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":95,"end":110},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":112,"end":116},"obj":"OrganismTaxon"},{"id":"T4","span":{"begin":187,"end":191},"obj":"OrganismTaxon"},{"id":"T5","span":{"begin":1635,"end":1639},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"1891767"},{"id":"A2","pred":"db_id","subj":"T2","obj":"1891767"},{"id":"A3","pred":"db_id","subj":"T3","obj":"1891767"},{"id":"A4","pred":"db_id","subj":"T4","obj":"1891767"},{"id":"A5","pred":"db_id","subj":"T5","obj":"1891767"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"GlyCosmos-GlycoEpitope","denotations":[{"id":"T1","span":{"begin":37,"end":46},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T2","span":{"begin":139,"end":148},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T3","span":{"begin":305,"end":314},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T4","span":{"begin":629,"end":638},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T5","span":{"begin":917,"end":926},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T6","span":{"begin":1093,"end":1102},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T7","span":{"begin":1171,"end":1180},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T8","span":{"begin":1275,"end":1284},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T9","span":{"begin":1443,"end":1452},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"},{"id":"T10","span":{"begin":1640,"end":1649},"obj":"http://purl.jp/bio/12/glyco/glycan#Glycan_epitope"}],"attributes":[{"id":"A1","pred":"glycoepitope_id","subj":"T1","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A2","pred":"glycoepitope_id","subj":"T2","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A3","pred":"glycoepitope_id","subj":"T3","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A4","pred":"glycoepitope_id","subj":"T4","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A5","pred":"glycoepitope_id","subj":"T5","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A6","pred":"glycoepitope_id","subj":"T6","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A7","pred":"glycoepitope_id","subj":"T7","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A8","pred":"glycoepitope_id","subj":"T8","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A9","pred":"glycoepitope_id","subj":"T9","obj":"http://www.glycoepitope.jp/epitopes/EP0020"},{"id":"A10","pred":"glycoepitope_id","subj":"T10","obj":"http://www.glycoepitope.jp/epitopes/EP0020"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"Anatomy-UBERON","denotations":[{"id":"T1","span":{"begin":68,"end":76},"obj":"Body_part"},{"id":"T2","span":{"begin":948,"end":956},"obj":"Body_part"},{"id":"T3","span":{"begin":1474,"end":1482},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"uberon_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"},{"id":"A2","pred":"uberon_id","subj":"T2","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"},{"id":"A3","pred":"uberon_id","subj":"T3","obj":"http://purl.obolibrary.org/obo/UBERON_0001130"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}

{"project":"HP-phenotype","denotations":[{"id":"T1","span":{"begin":124,"end":129},"obj":"Phenotype"}],"attributes":[{"id":"A1","pred":"hp_id","subj":"T1","obj":"HP:0002664"}],"namespaces":[{"prefix":"HP","uri":"http://purl.obolibrary.org/obo/HP_"}],"text":"The binding of simian virus 40 large T antigen to the polyphosphate backbone of nucleic acids.\nSimian virus 40 (SV40) large tumor antigen (T antigen), a phosphoprotein found in nuclei of SV40-infected and -transformed cells, binds nonspecifically to DNA. To study this mechanism the binding properties of T antigen to double-stranded (ds) and single-stranded (ss) DNA-cellulose as well as to phosphocellulose were compared. After incubation of [35S] methionine or [3H] leucine/[32 P] phosphate radioactively-labeled cell extracts at different pH values (6.0, 7.3, 9.0) with DNA- or phosphocellulose, bound and unbound species of T antigen were purified and analyzed by SDS-polyacrylamide gel electrophoresis for both the yield and the possible correlation with protein phosphorylation. T antigens bound with comparable affinities to ds- and ss-DNA-cellulose and phosphocellulose. These results suggest the binding of T antigen to the polyphosphate backbone of DNA as a molecular mechanism for its nonspecific binding. The evidence for this observation was supported by blocking the binding of T antigen to DNA-cellulose by divalent cations (Ca2+, Mg2+). 3H/32P ratios of T antigen obtained by double-labeling cells for various times imply that higher phosphorylated forms of T antigen bound more strongly to ds- and ss-DNA as well as to phosphocellulose. Thus, in the presence of cellular proteins and other components the binding activity of T antigen to the polyphosphate backbone of DNA seems to be positively correlated with its phosphorylation. These observations are consistent with the hypothesis that the binding affinities of SV40 T antigen to host cell DNA may be regulated by its phosphorylation."}