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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
1
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pubmed:dateCreated |
2007-1-12
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pubmed:abstractText |
High-fidelity chromosomal segregation requires the properly timed establishment of sister-chromatid cohesion mediated by the Cohesin complex, and its resolution at the metaphase-to-anaphase transition. We have examined cell-cycle progression in a yeast strain from which the origin recognition complex protein Orc2 was depleted after the assembly of prereplication complexes. We find that Orc2 depletion causes a delay in progression through mitosis, reflecting activation of both the DNA-damage and Mad2-spindle checkpoints. Surprisingly, sister-chromatid cohesion is impaired in Orc2-depleted cells, although Cohesin subunits are properly associated with chromatin. Reexpression of Orc2 in late G2/M phase restores chromatid cohesion. Finally, the targeting of Orc2 to a specific chromosomal locus suppresses premature sister-chromatid separation locally in a temperature-sensitive cohesin mutant. We conclude that ORC mediates sister-chromatid interaction on a pathway that is additive with Cohesin-mediated pairing.
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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/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/MAD2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ORC2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Origin Recognition Complex,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/cohesins,
http://linkedlifedata.com/resource/pubmed/chemical/structural maintenance of...
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0092-8674
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
12
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pubmed:volume |
128
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
85-99
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pubmed:dateRevised |
2008-11-7
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pubmed:meshHeading |
pubmed-meshheading:17218257-Acetyltransferases,
pubmed-meshheading:17218257-Cell Cycle Proteins,
pubmed-meshheading:17218257-Chromatids,
pubmed-meshheading:17218257-Chromatin,
pubmed-meshheading:17218257-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:17218257-Chromosome Pairing,
pubmed-meshheading:17218257-Chromosomes, Fungal,
pubmed-meshheading:17218257-DNA Damage,
pubmed-meshheading:17218257-DNA Replication,
pubmed-meshheading:17218257-G1 Phase,
pubmed-meshheading:17218257-Mitosis,
pubmed-meshheading:17218257-Mitotic Spindle Apparatus,
pubmed-meshheading:17218257-Models, Biological,
pubmed-meshheading:17218257-Nuclear Proteins,
pubmed-meshheading:17218257-Origin Recognition Complex,
pubmed-meshheading:17218257-Protein Binding,
pubmed-meshheading:17218257-Protein Transport,
pubmed-meshheading:17218257-Saccharomyces cerevisiae,
pubmed-meshheading:17218257-Saccharomyces cerevisiae Proteins
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pubmed:year |
2007
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pubmed:articleTitle |
The origin recognition complex functions in sister-chromatid cohesion in Saccharomyces cerevisiae.
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pubmed:affiliation |
Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058 Basel, Switzerland.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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