Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-2-28
pubmed:abstractText
Meiotic crossing-over is highly regulated such that each homolog pair typically receives at least one crossover (assurance) and adjacent crossovers are widely spaced (interference). Here we provide evidence that interference and assurance are mechanistically distinct processes that are separated by mutations in a new ZMM (Zip, Msh, Mer) protein from Saccharomyces cerevisiae, Spo16. Like other zmm mutants, spo16 cells have defects in both crossing-over and synaptonemal complex formation. Unlike in previously characterized zmm mutants, the residual crossovers in spo16 cells show interference comparable to that in the wild type. Spo16 interacts with a second ZMM protein, Spo22 (also known as Zip4), and spo22 mutants also show normal interference. Notably, assembly of the MutS homologs Msh4 and Msh5 on chromosomes occurs in both spo16 and spo22, but not in other zmm mutants. We suggest that crossover interference requires the normal assembly of recombination complexes containing Msh4 and Msh5 but does not require Spo16- and Spo22-dependent extension of synaptonemal complexes. In contrast, crossover assurance requires all ZMM proteins and full-length synaptonemal complexes.
pubmed:grant
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
1546-1718
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
299-309
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed-meshheading:18297071-Chromosomal Proteins, Non-Histone, pubmed-meshheading:18297071-Chromosome Pairing, pubmed-meshheading:18297071-Chromosomes, Fungal, pubmed-meshheading:18297071-Crossing Over, Genetic, pubmed-meshheading:18297071-DNA-Binding Proteins, pubmed-meshheading:18297071-Dimerization, pubmed-meshheading:18297071-In Situ Hybridization, Fluorescence, pubmed-meshheading:18297071-Meiosis, pubmed-meshheading:18297071-Microtubule-Associated Proteins, pubmed-meshheading:18297071-Models, Biological, pubmed-meshheading:18297071-Mutant Proteins, pubmed-meshheading:18297071-Nuclear Proteins, pubmed-meshheading:18297071-Organisms, Genetically Modified, pubmed-meshheading:18297071-Protein Binding, pubmed-meshheading:18297071-Saccharomyces cerevisiae, pubmed-meshheading:18297071-Saccharomyces cerevisiae Proteins, pubmed-meshheading:18297071-Synaptonemal Complex, pubmed-meshheading:18297071-Tissue Distribution, pubmed-meshheading:18297071-Ubiquitin-Protein Ligases
pubmed:year
2008
pubmed:articleTitle
Crossover assurance and crossover interference are distinctly regulated by the ZMM proteins during yeast meiosis.
pubmed:affiliation
Institute for Protein Research, Osaka University, Suita 565-0871, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't, Research Support, N.I.H., Extramural