Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
1998-7-9
pubmed:abstractText
Cohesion between sister chromatids during G2 and M phases depends on the "cohesin" protein Scc1p (Mcd1p). Loss of cohesion at the metaphase to anaphase transition is accompanied by Scc1p's dissociation from chromatids, which depends on proteolysis of Pds1p mediated by a ubiquitin protein ligase called the anaphase promoting complex (APC). We show that destruction of Pds1p is the APC's sole role in triggering Scc1p's dissociation from chromatids and that Pds1p forms a stable complex with a 180 kDa protein called Esp1p, which is essential for the dissociation of Scc1p from sister chromatids and for their separation. We propose that the APC promotes sister separation not by destroying cohesins but instead by liberating the "sister-separating" Esp1 protein from its inhibitor Pds1p.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone, http://linkedlifedata.com/resource/pubmed/chemical/Endopeptidases, http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ligases, http://linkedlifedata.com/resource/pubmed/chemical/MCD1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins, http://linkedlifedata.com/resource/pubmed/chemical/PDS1 protein, S cerevisiae, http://linkedlifedata.com/resource/pubmed/chemical/Phosphoproteins, http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligase Complexes, http://linkedlifedata.com/resource/pubmed/chemical/Ubiquitin-Protein Ligases, http://linkedlifedata.com/resource/pubmed/chemical/anaphase-promoting complex
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
93
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1067-76
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:9635435-Anaphase, pubmed-meshheading:9635435-Cell Cycle Proteins, pubmed-meshheading:9635435-Cell Nucleus, pubmed-meshheading:9635435-Chromatids, pubmed-meshheading:9635435-Chromosomal Proteins, Non-Histone, pubmed-meshheading:9635435-Chromosomes, Fungal, pubmed-meshheading:9635435-Endopeptidases, pubmed-meshheading:9635435-Fungal Proteins, pubmed-meshheading:9635435-Ligases, pubmed-meshheading:9635435-Metaphase, pubmed-meshheading:9635435-Molecular Weight, pubmed-meshheading:9635435-Mutation, pubmed-meshheading:9635435-Nuclear Proteins, pubmed-meshheading:9635435-Phosphoproteins, pubmed-meshheading:9635435-Saccharomyces cerevisiae, pubmed-meshheading:9635435-Saccharomyces cerevisiae Proteins, pubmed-meshheading:9635435-Ubiquitin-Protein Ligase Complexes, pubmed-meshheading:9635435-Ubiquitin-Protein Ligases
pubmed:year
1998
pubmed:articleTitle
An ESP1/PDS1 complex regulates loss of sister chromatid cohesion at the metaphase to anaphase transition in yeast.
pubmed:affiliation
Research Institute of Molecular Pathology, Vienna, Austria.
pubmed:publicationType
Journal Article