PubMed:15574802 JSON TXT

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Glycosmos6-MAT

{"project":"Glycosmos6-MAT","denotations":[{"id":"T1","span":{"begin":442,"end":453},"obj":"http://purl.obolibrary.org/obo/MAT_0000190"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

sentences

{"project":"sentences","denotations":[{"id":"TextSentencer_T1","span":{"begin":0,"end":107},"obj":"Sentence"},{"id":"TextSentencer_T2","span":{"begin":108,"end":258},"obj":"Sentence"},{"id":"TextSentencer_T3","span":{"begin":259,"end":461},"obj":"Sentence"},{"id":"TextSentencer_T4","span":{"begin":462,"end":654},"obj":"Sentence"},{"id":"TextSentencer_T5","span":{"begin":655,"end":776},"obj":"Sentence"},{"id":"TextSentencer_T6","span":{"begin":777,"end":863},"obj":"Sentence"},{"id":"TextSentencer_T7","span":{"begin":864,"end":938},"obj":"Sentence"},{"id":"TextSentencer_T8","span":{"begin":939,"end":1057},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":107},"obj":"Sentence"},{"id":"T2","span":{"begin":108,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":461},"obj":"Sentence"},{"id":"T4","span":{"begin":462,"end":654},"obj":"Sentence"},{"id":"T5","span":{"begin":655,"end":776},"obj":"Sentence"},{"id":"T6","span":{"begin":777,"end":863},"obj":"Sentence"},{"id":"T7","span":{"begin":864,"end":938},"obj":"Sentence"},{"id":"T8","span":{"begin":939,"end":1057},"obj":"Sentence"},{"id":"T1","span":{"begin":0,"end":107},"obj":"Sentence"},{"id":"T2","span":{"begin":108,"end":258},"obj":"Sentence"},{"id":"T3","span":{"begin":259,"end":461},"obj":"Sentence"},{"id":"T4","span":{"begin":462,"end":654},"obj":"Sentence"},{"id":"T5","span":{"begin":655,"end":776},"obj":"Sentence"},{"id":"T6","span":{"begin":777,"end":863},"obj":"Sentence"},{"id":"T7","span":{"begin":864,"end":938},"obj":"Sentence"},{"id":"T8","span":{"begin":939,"end":1057},"obj":"Sentence"}],"namespaces":[{"prefix":"_base","uri":"http://pubannotation.org/ontology/tao.owl#"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

GlycoBiology-PACDB

{"project":"GlycoBiology-PACDB","denotations":[{"id":"_T1","span":{"begin":139,"end":159},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC257,LEC564"},{"id":"_T2","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC295,LEC417"},{"id":"_T3","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC157,LEC407"},{"id":"_T4","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC754"},{"id":"_T5","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC243,LEC640"},{"id":"_T6","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC002,LEC056,LEC062,LEC069,LEC081,LEC111,LEC133,LEC171,LEC177,LEC187,LEC211,LEC242,LEC252,LEC258,LEC259,LEC260,LEC262,LEC369,LEC377,LEC422,LEC442,LEC448,LEC450,LEC451,LEC454,LEC472,LEC492,LEC620"},{"id":"_T7","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC487"},{"id":"_T8","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC244,LEC256,LEC354"},{"id":"_T9","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC054,LEC058,LEC073,LEC082,LEC091,LEC103,LEC109,LEC110,LEC123,LEC158,LEC179,LEC198,LEC205,LEC222,LEC223,LEC224,LEC225,LEC232,LEC298,LEC357,LEC378,LEC383,LEC388,LEC389,LEC397,LEC401,LEC410,LEC452"},{"id":"_T10","span":{"begin":637,"end":653},"obj":"http://acgg.asia/db/diseases/pacdb/lec?ids=LEC636"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

uniprot-mouse

{"project":"uniprot-mouse","denotations":[{"id":"T1","span":{"begin":171,"end":174},"obj":"http://www.uniprot.org/uniprot/Q9CQ60"},{"id":"T2","span":{"begin":290,"end":293},"obj":"http://www.uniprot.org/uniprot/Q9CQ60"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

GlycoBiology-NCBITAXON

GO-BP

{"project":"GO-BP","denotations":[{"id":"T1","span":{"begin":85,"end":106},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T2","span":{"begin":176,"end":197},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T3","span":{"begin":754,"end":775},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T4","span":{"begin":1010,"end":1031},"obj":"http://purl.obolibrary.org/obo/GO_0006486"},{"id":"T5","span":{"begin":93,"end":106},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T6","span":{"begin":184,"end":197},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T7","span":{"begin":225,"end":238},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T8","span":{"begin":522,"end":535},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T9","span":{"begin":594,"end":607},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T10","span":{"begin":762,"end":775},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T11","span":{"begin":924,"end":937},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T12","span":{"begin":1018,"end":1031},"obj":"http://purl.obolibrary.org/obo/GO_0070085"},{"id":"T13","span":{"begin":171,"end":174},"obj":"http://purl.obolibrary.org/obo/GO_0004598"},{"id":"T14","span":{"begin":290,"end":293},"obj":"http://purl.obolibrary.org/obo/GO_0004598"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

GO-CC

{"project":"GO-CC","denotations":[{"id":"T1","span":{"begin":897,"end":906},"obj":"http://purl.obolibrary.org/obo/GO_0042597"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

GlycoBiology-MAT

{"project":"GlycoBiology-MAT","denotations":[{"id":"T1","span":{"begin":129,"end":138},"obj":"http://purl.obolibrary.org/obo/MAT_0000191"},{"id":"T2","span":{"begin":442,"end":453},"obj":"http://purl.obolibrary.org/obo/MAT_0000190"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

Anatomy-MAT

{"project":"Anatomy-MAT","denotations":[{"id":"T1","span":{"begin":442,"end":453},"obj":"Body_part"}],"attributes":[{"id":"A1","pred":"mat_id","subj":"T1","obj":"http://purl.obolibrary.org/obo/MAT_0000190"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}

NCBITAXON

{"project":"NCBITAXON","denotations":[{"id":"T1","span":{"begin":139,"end":159},"obj":"OrganismTaxon"},{"id":"T2","span":{"begin":637,"end":653},"obj":"OrganismTaxon"},{"id":"T3","span":{"begin":661,"end":671},"obj":"OrganismTaxon"}],"attributes":[{"id":"A1","pred":"db_id","subj":"T1","obj":"197"},{"id":"A2","pred":"db_id","subj":"T2","obj":"562"},{"id":"A3","pred":"db_id","subj":"T3","obj":"2759"}],"text":"The N-X-S/T consensus sequence is required but not sufficient for bacterial N-linked protein glycosylation.\nIn the Gram-negative bacterium Campylobacter jejuni there is a pgl (protein glycosylation) locus-dependent general N-glycosylation system of proteins. One of the proteins encoded by pgl locus, PglB, a homolog of the eukaryotic oligosaccharyltransferase component Stt3p, is proposed to function as an oligosaccharyltransferase in this prokaryotic system. The sequence requirements of the acceptor polypeptide for N-glycosylation were analyzed by reverse genetics using the reconstituted glycosylation of the model protein AcrA in Escherichia coli. As in eukaryotes, the N-X-S/T sequon is an essential but not a sufficient determinant for N-linked protein glycosylation. This conclusion was supported by the analysis of a novel C. jejuni glycoprotein, HisJ. Export of the polypeptide to the periplasm was required for glycosylation. Our data support the hypothesis that eukaryotic and bacterial N-linked protein glycosylation are homologous processes."}