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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
2
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pubmed:dateCreated |
2000-9-14
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pubmed:abstractText |
In budding yeast, absence of the meiosis-specific Zip3 protein (also known as Cst9) causes synaptonemal complex formation to be delayed and incomplete. The Zip3 protein colocalizes with Zip2 at discrete foci on meiotic chromosomes, corresponding to the sites where synapsis initiates. Observations suggest that Zip3 promotes synapsis by recruiting the Zip2 protein to chromosomes and/or stabilizing the association of Zip2 with chromosomes. Zip3 interacts with a number of gene products involved in meiotic recombination, including proteins that act at both early (Mre11, Rad51, and Rad57) and late (Msh4 and Msh5) steps in the exchange process. We speculate that Zip3 is a component of recombination nodules and serves to link the initiation of synapsis to meiotic recombination.
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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/Adenosine Triphosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Repair Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Endodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Enzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Exodeoxyribonucleases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/MRE11 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MSH4 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/MSH5 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RAD51 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/RAD57 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Rad51 Recombinase,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Zip1 protein, S cerevisiae
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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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 |
21
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pubmed:volume |
102
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
245-55
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:10943844-Adenosine Triphosphatases,
pubmed-meshheading:10943844-Cell Nucleus,
pubmed-meshheading:10943844-Chromosomes, Fungal,
pubmed-meshheading:10943844-Crossing Over, Genetic,
pubmed-meshheading:10943844-DNA Repair Enzymes,
pubmed-meshheading:10943844-DNA-Binding Proteins,
pubmed-meshheading:10943844-Endodeoxyribonucleases,
pubmed-meshheading:10943844-Enzymes,
pubmed-meshheading:10943844-Exodeoxyribonucleases,
pubmed-meshheading:10943844-Fungal Proteins,
pubmed-meshheading:10943844-Meiosis,
pubmed-meshheading:10943844-Nondisjunction, Genetic,
pubmed-meshheading:10943844-Nuclear Proteins,
pubmed-meshheading:10943844-Rad51 Recombinase,
pubmed-meshheading:10943844-Recombination, Genetic,
pubmed-meshheading:10943844-Saccharomyces cerevisiae,
pubmed-meshheading:10943844-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:10943844-Synaptonemal Complex
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pubmed:year |
2000
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pubmed:articleTitle |
Zip3 provides a link between recombination enzymes and synaptonemal complex proteins.
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pubmed:affiliation |
Howard Hughes Medical Institute, Department of Molecular, Cellular and Developmental Biology, Yale University, New Haven, Connecticut 06520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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