PubMed:8065331 JSONTXT

{"project":"DisGeNET","denotations":[{"id":"T0","span":{"begin":57,"end":80},"obj":"gene:3131"},{"id":"T1","span":{"begin":104,"end":132},"obj":"disease:C0023449"},{"id":"T2","span":{"begin":57,"end":80},"obj":"gene:3131"},{"id":"T3","span":{"begin":104,"end":132},"obj":"disease:C1961102"},{"id":"T4","span":{"begin":416,"end":419},"obj":"gene:6929"},{"id":"T5","span":{"begin":180,"end":209},"obj":"disease:C0023449"},{"id":"T6","span":{"begin":609,"end":612},"obj":"gene:3131"},{"id":"T7","span":{"begin":661,"end":670},"obj":"disease:C0023418"}],"relations":[{"id":"R1","pred":"associated_with","subj":"T0","obj":"T1"},{"id":"R2","pred":"associated_with","subj":"T2","obj":"T3"},{"id":"R3","pred":"associated_with","subj":"T4","obj":"T5"},{"id":"R4","pred":"associated_with","subj":"T6","obj":"T7"}],"namespaces":[{"prefix":"gene","uri":"http://www.ncbi.nlm.nih.gov/gene/"},{"prefix":"disease","uri":"http://purl.bioontology.org/ontology/MEDLINEPLUS/"}],"text":"DNA-binding and transcriptional regulatory properties of hepatic leukemia factor (HLF) and the t(17;19) acute lymphoblastic leukemia chimera E2A-HLF.\nThe t(17;19) translocation in acute lymphoblastic leukemias results in creation of E2A-hepatic leukemia factor (HLF) chimeric proteins that contain the DNA-binding and protein dimerization domains of the basic leucine zipper (bZIP) protein HLF fused to a portion of E2A proteins with transcriptional activation properties. An in vitro binding site selection procedure was used to determine DNA sequences preferentially bound by wild-type HLF and chimeric E2A-HLF proteins isolated from various t(17;19)-bearing leukemias. All were found to selectively bind the consensus sequence 5'-GTTACGTAAT-3' with high affinity. Wild-type and chimeric HLF proteins also bound closely related sites identified previously for bZIP proteins of both the proline- and acidic amino acid-rich (PAR) and C/EBP subfamilies; however, E2A-HLF proteins were significantly less tolerant of certain deviations from the HLF consensus binding site. These differences were directly attributable to loss of an HLF ancillary DNA-binding domain in all E2A-HLF chimeras and were further exacerbated by a zipper mutation in one isolate. Both wild-type and chimeric HLF proteins displayed transcriptional activator properties in lymphoid and nonlymphoid cells on reporter genes containing HLF or C/EBP consensus binding sites. But on reporter genes with nonoptimal binding sites, their transcriptional properties diverged and E2A-HLF competitively inhibited activation by wild-type PAR proteins. These findings establish a spectrum of binding site-specific transcriptional properties for E2A-HLF which may preferentially activate expression of select subordinate genes as a homodimer and potentially antagonize expression of others through heteromeric interactions."}

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{"project":"DisGeNET5_gene_disease","denotations":[{"id":"8065331-1#266#269#gene6929","span":{"begin":416,"end":419},"obj":"gene6929"},{"id":"8065331-1#30#59#diseaseC0023449","span":{"begin":180,"end":209},"obj":"diseaseC0023449"},{"id":"8065331-2#136#139#gene3131","span":{"begin":609,"end":612},"obj":"gene3131"},{"id":"8065331-2#188#197#diseaseC0023418","span":{"begin":661,"end":670},"obj":"diseaseC0023418"}],"relations":[{"id":"266#269#gene692930#59#diseaseC0023449","pred":"associated_with","subj":"8065331-1#266#269#gene6929","obj":"8065331-1#30#59#diseaseC0023449"},{"id":"136#139#gene3131188#197#diseaseC0023418","pred":"associated_with","subj":"8065331-2#136#139#gene3131","obj":"8065331-2#188#197#diseaseC0023418"}],"text":"DNA-binding and transcriptional regulatory properties of hepatic leukemia factor (HLF) and the t(17;19) acute lymphoblastic leukemia chimera E2A-HLF.\nThe t(17;19) translocation in acute lymphoblastic leukemias results in creation of E2A-hepatic leukemia factor (HLF) chimeric proteins that contain the DNA-binding and protein dimerization domains of the basic leucine zipper (bZIP) protein HLF fused to a portion of E2A proteins with transcriptional activation properties. An in vitro binding site selection procedure was used to determine DNA sequences preferentially bound by wild-type HLF and chimeric E2A-HLF proteins isolated from various t(17;19)-bearing leukemias. All were found to selectively bind the consensus sequence 5'-GTTACGTAAT-3' with high affinity. Wild-type and chimeric HLF proteins also bound closely related sites identified previously for bZIP proteins of both the proline- and acidic amino acid-rich (PAR) and C/EBP subfamilies; however, E2A-HLF proteins were significantly less tolerant of certain deviations from the HLF consensus binding site. These differences were directly attributable to loss of an HLF ancillary DNA-binding domain in all E2A-HLF chimeras and were further exacerbated by a zipper mutation in one isolate. Both wild-type and chimeric HLF proteins displayed transcriptional activator properties in lymphoid and nonlymphoid cells on reporter genes containing HLF or C/EBP consensus binding sites. But on reporter genes with nonoptimal binding sites, their transcriptional properties diverged and E2A-HLF competitively inhibited activation by wild-type PAR proteins. These findings establish a spectrum of binding site-specific transcriptional properties for E2A-HLF which may preferentially activate expression of select subordinate genes as a homodimer and potentially antagonize expression of others through heteromeric interactions."}

{"project":"pubmed-sentences-benchmark","denotations":[{"id":"S1","span":{"begin":0,"end":149},"obj":"Sentence"},{"id":"S2","span":{"begin":150,"end":472},"obj":"Sentence"},{"id":"S3","span":{"begin":473,"end":671},"obj":"Sentence"},{"id":"S4","span":{"begin":672,"end":766},"obj":"Sentence"},{"id":"S5","span":{"begin":767,"end":1070},"obj":"Sentence"},{"id":"S6","span":{"begin":1071,"end":1252},"obj":"Sentence"},{"id":"S7","span":{"begin":1253,"end":1441},"obj":"Sentence"},{"id":"S8","span":{"begin":1442,"end":1610},"obj":"Sentence"},{"id":"S9","span":{"begin":1611,"end":1880},"obj":"Sentence"}],"text":"DNA-binding and transcriptional regulatory properties of hepatic leukemia factor (HLF) and the t(17;19) acute lymphoblastic leukemia chimera E2A-HLF.\nThe t(17;19) translocation in acute lymphoblastic leukemias results in creation of E2A-hepatic leukemia factor (HLF) chimeric proteins that contain the DNA-binding and protein dimerization domains of the basic leucine zipper (bZIP) protein HLF fused to a portion of E2A proteins with transcriptional activation properties. An in vitro binding site selection procedure was used to determine DNA sequences preferentially bound by wild-type HLF and chimeric E2A-HLF proteins isolated from various t(17;19)-bearing leukemias. All were found to selectively bind the consensus sequence 5'-GTTACGTAAT-3' with high affinity. Wild-type and chimeric HLF proteins also bound closely related sites identified previously for bZIP proteins of both the proline- and acidic amino acid-rich (PAR) and C/EBP subfamilies; however, E2A-HLF proteins were significantly less tolerant of certain deviations from the HLF consensus binding site. These differences were directly attributable to loss of an HLF ancillary DNA-binding domain in all E2A-HLF chimeras and were further exacerbated by a zipper mutation in one isolate. Both wild-type and chimeric HLF proteins displayed transcriptional activator properties in lymphoid and nonlymphoid cells on reporter genes containing HLF or C/EBP consensus binding sites. But on reporter genes with nonoptimal binding sites, their transcriptional properties diverged and E2A-HLF competitively inhibited activation by wild-type PAR proteins. These findings establish a spectrum of binding site-specific transcriptional properties for E2A-HLF which may preferentially activate expression of select subordinate genes as a homodimer and potentially antagonize expression of others through heteromeric interactions."}

{"project":"genia-medco-coref","denotations":[{"id":"C1","span":{"begin":0,"end":11},"obj":"NP"},{"id":"C2","span":{"begin":91,"end":148},"obj":"NP"},{"id":"C3","span":{"begin":233,"end":284},"obj":"NP"},{"id":"C4","span":{"begin":285,"end":289},"obj":"NP"},{"id":"C5","span":{"begin":298,"end":313},"obj":"NP"},{"id":"C6","span":{"begin":416,"end":428},"obj":"NP"},{"id":"C8","span":{"begin":596,"end":621},"obj":"NP"},{"id":"C7","span":{"begin":578,"end":621},"obj":"NP"},{"id":"C9","span":{"begin":672,"end":675},"obj":"NP"},{"id":"C10","span":{"begin":767,"end":802},"obj":"NP"},{"id":"C11","span":{"begin":962,"end":978},"obj":"NP"},{"id":"C12","span":{"begin":1166,"end":1186},"obj":"NP"},{"id":"C13","span":{"begin":1253,"end":1293},"obj":"NP"},{"id":"C14","span":{"begin":1378,"end":1440},"obj":"NP"},{"id":"C15","span":{"begin":1449,"end":1493},"obj":"NP"},{"id":"C16","span":{"begin":1495,"end":1500},"obj":"NP"},{"id":"C17","span":{"begin":1541,"end":1548},"obj":"NP"},{"id":"C19","span":{"begin":1703,"end":1710},"obj":"NP"},{"id":"C18","span":{"begin":1636,"end":1710},"obj":"NP"},{"id":"C20","span":{"begin":1711,"end":1716},"obj":"NP"}],"relations":[{"id":"R1","pred":"coref-ident","subj":"C3","obj":"C2"},{"id":"R2","pred":"coref-relat","subj":"C4","obj":"C3"},{"id":"R3","pred":"coref-ident","subj":"C5","obj":"C1"},{"id":"R4","pred":"coref-ident","subj":"C6","obj":"C3"},{"id":"R5","pred":"coref-ident","subj":"C8","obj":"C3"},{"id":"R6","pred":"coref-ident","subj":"C9","obj":"C7"},{"id":"R7","pred":"coref-ident","subj":"C10","obj":"C7"},{"id":"R8","pred":"coref-ident","subj":"C11","obj":"C10"},{"id":"R9","pred":"coref-ident","subj":"C13","obj":"C10"},{"id":"R10","pred":"coref-ident","subj":"C15","obj":"C14"},{"id":"R11","pred":"coref-pron","subj":"C16","obj":"C12"},{"id":"R12","pred":"coref-ident","subj":"C17","obj":"C12"},{"id":"R13","pred":"coref-ident","subj":"C19","obj":"C17"},{"id":"R14","pred":"coref-relat","subj":"C20","obj":"C18"}],"text":"DNA-binding and transcriptional regulatory properties of hepatic leukemia factor (HLF) and the t(17;19) acute lymphoblastic leukemia chimera E2A-HLF.\nThe t(17;19) translocation in acute lymphoblastic leukemias results in creation of E2A-hepatic leukemia factor (HLF) chimeric proteins that contain the DNA-binding and protein dimerization domains of the basic leucine zipper (bZIP) protein HLF fused to a portion of E2A proteins with transcriptional activation properties. An in vitro binding site selection procedure was used to determine DNA sequences preferentially bound by wild-type HLF and chimeric E2A-HLF proteins isolated from various t(17;19)-bearing leukemias. All were found to selectively bind the consensus sequence 5'-GTTACGTAAT-3' with high affinity. Wild-type and chimeric HLF proteins also bound closely related sites identified previously for bZIP proteins of both the proline- and acidic amino acid-rich (PAR) and C/EBP subfamilies; however, E2A-HLF proteins were significantly less tolerant of certain deviations from the HLF consensus binding site. These differences were directly attributable to loss of an HLF ancillary DNA-binding domain in all E2A-HLF chimeras and were further exacerbated by a zipper mutation in one isolate. Both wild-type and chimeric HLF proteins displayed transcriptional activator properties in lymphoid and nonlymphoid cells on reporter genes containing HLF or C/EBP consensus binding sites. But on reporter genes with nonoptimal binding sites, their transcriptional properties diverged and E2A-HLF competitively inhibited activation by wild-type PAR proteins. These findings establish a spectrum of binding site-specific transcriptional properties for E2A-HLF which may preferentially activate expression of select subordinate genes as a homodimer and potentially antagonize expression of others through heteromeric interactions."}

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An in vitro binding site selection procedure was used to determine DNA sequences preferentially bound by wild-type HLF and chimeric E2A-HLF proteins isolated from various t(17;19)-bearing leukemias. All were found to selectively bind the consensus sequence 5'-GTTACGTAAT-3' with high affinity. Wild-type and chimeric HLF proteins also bound closely related sites identified previously for bZIP proteins of both the proline- and acidic amino acid-rich (PAR) and C/EBP subfamilies; however, E2A-HLF proteins were significantly less tolerant of certain deviations from the HLF consensus binding site. These differences were directly attributable to loss of an HLF ancillary DNA-binding domain in all E2A-HLF chimeras and were further exacerbated by a zipper mutation in one isolate. Both wild-type and chimeric HLF proteins displayed transcriptional activator properties in lymphoid and nonlymphoid cells on reporter genes containing HLF or C/EBP consensus binding sites. But on reporter genes with nonoptimal binding sites, their transcriptional properties diverged and E2A-HLF competitively inhibited activation by wild-type PAR proteins. These findings establish a spectrum of binding site-specific transcriptional properties for E2A-HLF which may preferentially activate expression of select subordinate genes as a homodimer and potentially antagonize expression of others through heteromeric interactions."}