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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
38
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pubmed:dateCreated |
2001-9-17
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pubmed:abstractText |
Conjugation of the small ubiquitin-like modifier SUMO-1/SMT3C/Sentrin-1 to proteins in vitro is dependent on a heterodimeric E1 (SAE1/SAE2) and an E2 (Ubc9). Although SUMO-2/SMT3A/Sentrin-3 and SUMO-3/SMT3B/Sentrin-2 share 50% sequence identity with SUMO-1, they are functionally distinct. Inspection of the SUMO-2 and SUMO-3 sequences indicates that they both contain the sequence psiKXE, which represents the consensus SUMO modification site. As a consequence SAE1/SAE2 and Ubc9 catalyze the formation of polymeric chains of SUMO-2 and SUMO-3 on protein substrates in vitro, and SUMO-2 chains are detected in vivo. The ability to form polymeric chains is not shared by SUMO-1, and although all SUMO species use the same conjugation machinery, modification by SUMO-1 and SUMO-2/-3 may have distinct functional consequences.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Biopolymers,
http://linkedlifedata.com/resource/pubmed/chemical/CBC2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Endonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Ligases,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Cap-Binding Protein Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/SAE2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO2 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/SUMO3 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Small Ubiquitin-Related Modifier...,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Conjugating Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitins,
http://linkedlifedata.com/resource/pubmed/chemical/ubiquitin-conjugating enzyme UBC9
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0021-9258
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
21
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
35368-74
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11451954-Amino Acid Sequence,
pubmed-meshheading:11451954-Base Sequence,
pubmed-meshheading:11451954-Biopolymers,
pubmed-meshheading:11451954-Cell Line,
pubmed-meshheading:11451954-DNA Primers,
pubmed-meshheading:11451954-Endonucleases,
pubmed-meshheading:11451954-Fungal Proteins,
pubmed-meshheading:11451954-Humans,
pubmed-meshheading:11451954-Ligases,
pubmed-meshheading:11451954-Lysine,
pubmed-meshheading:11451954-Molecular Sequence Data,
pubmed-meshheading:11451954-Nuclear Cap-Binding Protein Complex,
pubmed-meshheading:11451954-Phosphoproteins,
pubmed-meshheading:11451954-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11451954-Sequence Homology, Amino Acid,
pubmed-meshheading:11451954-Small Ubiquitin-Related Modifier Proteins,
pubmed-meshheading:11451954-Substrate Specificity,
pubmed-meshheading:11451954-Ubiquitin-Conjugating Enzymes,
pubmed-meshheading:11451954-Ubiquitins
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pubmed:year |
2001
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pubmed:articleTitle |
Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9.
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pubmed:affiliation |
Institute of Biomolecular Sciences, University of St. Andrews, North Haugh, St. Andrews KY16 5ST, United Kingdom.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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