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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5888
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pubmed:dateCreated |
2008-7-25
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pubmed:abstractText |
Chromosome segregation, transcriptional regulation, and repair of DNA double-strand breaks require the cohesin protein complex. Cohesin holds the replicated chromosomes (sister chromatids) together to mediate sister chromatid cohesion. The mechanism of how cohesion is established is unknown. We found that in budding yeast, the head domain of the Smc3p subunit of cohesin is acetylated by the Eco1p acetyltransferase at two evolutionarily conserved residues, promoting the chromatin-bound cohesin to tether sister chromatids. Smc3p acetylation is induced in S phase after the chromatin loading of cohesin and is suppressed in G(1) and G(2)/M. Smc3 head acetylation and its cell cycle regulation provide important insights into the biology and mechanism of cohesion establishment.
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pubmed:grant |
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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/Acetyltransferases,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Chondroitin Sulfate Proteoglycans,
http://linkedlifedata.com/resource/pubmed/chemical/Chromatin,
http://linkedlifedata.com/resource/pubmed/chemical/Chromosomal Proteins, Non-Histone,
http://linkedlifedata.com/resource/pubmed/chemical/ECO1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Lysine,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/SMC3 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1095-9203
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
25
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pubmed:volume |
321
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
566-9
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pubmed:dateRevised |
2010-11-18
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pubmed:meshHeading |
pubmed-meshheading:18653894-Acetylation,
pubmed-meshheading:18653894-Acetyltransferases,
pubmed-meshheading:18653894-Amino Acid Sequence,
pubmed-meshheading:18653894-Amino Acid Substitution,
pubmed-meshheading:18653894-Cell Cycle Proteins,
pubmed-meshheading:18653894-Cell Division,
pubmed-meshheading:18653894-Chondroitin Sulfate Proteoglycans,
pubmed-meshheading:18653894-Chromatids,
pubmed-meshheading:18653894-Chromatin,
pubmed-meshheading:18653894-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:18653894-Chromosomes, Fungal,
pubmed-meshheading:18653894-G1 Phase,
pubmed-meshheading:18653894-G2 Phase,
pubmed-meshheading:18653894-Immunoprecipitation,
pubmed-meshheading:18653894-Lysine,
pubmed-meshheading:18653894-Molecular Sequence Data,
pubmed-meshheading:18653894-Mutation,
pubmed-meshheading:18653894-Nuclear Proteins,
pubmed-meshheading:18653894-Protein Structure, Tertiary,
pubmed-meshheading:18653894-S Phase,
pubmed-meshheading:18653894-Saccharomyces cerevisiae,
pubmed-meshheading:18653894-Saccharomyces cerevisiae Proteins
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pubmed:year |
2008
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pubmed:articleTitle |
A molecular determinant for the establishment of sister chromatid cohesion.
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pubmed:affiliation |
Howard Hughes Medical Institute and Department of Embryology, Carnegie Institution, 3520 San Martin Drive, Baltimore, MD 21218, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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