Source:http://linkedlifedata.com/resource/pubmed/id/16740482
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
6
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pubmed:dateCreated |
2006-6-2
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pubmed:abstractText |
We have characterized Zip4 (a.k.a. Spo22), a meiosis-specific protein essential for chromosome synapsis in budding yeast. In the absence of Zip4, the synaptonemal complex protein Zip1 fails to polymerize along chromosomes. Zip2 and Zip3 are previously characterized components of the synapsis initiation complex. Zip4 forms a functional unit with Zip2 that is distinct from Zip3. Zip2 and Zip4 are mutually dependent for their chromosomal localization; in polycomplexes, the pattern of Zip2/Zip4 localization is distinct from that of Zip3. Crossing-over is decreased in the zip4 mutant (as in zip1, zip2, and zip3); the remaining crossovers are largely dependent on a parallel pathway utilizing Mms4. zip4 displays a novel phenotype: negative crossover interference, meaning that crossovers tend to cluster. This clustering depends on Zip1. Our results suggest an interaction between crossover pathways such that a protein (Zip1) acting in one pathway influences the distribution of crossovers promoted by a parallel (Mms4-dependent) pathway.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1534-5807
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
809-19
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:16740482-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:16740482-Crossing Over, Genetic,
pubmed-meshheading:16740482-Meiosis,
pubmed-meshheading:16740482-Mutation,
pubmed-meshheading:16740482-Saccharomyces cerevisiae,
pubmed-meshheading:16740482-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:16740482-Synaptonemal Complex
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pubmed:year |
2006
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pubmed:articleTitle |
The meiosis-specific zip4 protein regulates crossover distribution by promoting synaptonemal complex formation together with zip2.
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pubmed:affiliation |
Howard Hughes Medical Institute, Yale University, New Haven, Connecticut 06520, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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