rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
7
|
pubmed:dateCreated |
2005-2-8
|
pubmed:abstractText |
The centromere-specific histone H3 variant CENP-A plays a crucial role in kinetochore specification and assembly. We chose a genetic approach to identify interactors of the Drosophila CENP-A homolog CID. Overexpression of cid in the proliferating eye imaginal disk results in a rough eye phenotype, which is dependent on the ability of the overexpressed protein to localize to the kinetochore. A screen for modifiers of the rough eye phenotype identified mutations in the Drosophila condensin subunit gene Cap-G as interactors. Yeast two-hybrid experiments also reveal an interaction between CID and Cap-G. While chromosome condensation in Cap-G mutant embryos appears largely unaffected, massive defects in sister chromatid segregation occur during mitosis. Taken together, our results suggest a link between the chromatin condensation machinery and kinetochore structure.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Feb
|
pubmed:issn |
0009-5915
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:volume |
113
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
350-61
|
pubmed:dateRevised |
2006-11-15
|
pubmed:meshHeading |
pubmed-meshheading:15592865-Adenosine Triphosphatases,
pubmed-meshheading:15592865-Animals,
pubmed-meshheading:15592865-Centromere,
pubmed-meshheading:15592865-Chromosome Segregation,
pubmed-meshheading:15592865-DNA-Binding Proteins,
pubmed-meshheading:15592865-Drosophila Proteins,
pubmed-meshheading:15592865-Drosophila melanogaster,
pubmed-meshheading:15592865-Embryo, Nonmammalian,
pubmed-meshheading:15592865-Female,
pubmed-meshheading:15592865-Histones,
pubmed-meshheading:15592865-Kinetochores,
pubmed-meshheading:15592865-Male,
pubmed-meshheading:15592865-Microfilament Proteins,
pubmed-meshheading:15592865-Mitosis,
pubmed-meshheading:15592865-Multiprotein Complexes,
pubmed-meshheading:15592865-Mutation,
pubmed-meshheading:15592865-Protein Binding,
pubmed-meshheading:15592865-Protein Subunits,
pubmed-meshheading:15592865-Saccharomyces cerevisiae,
pubmed-meshheading:15592865-Sister Chromatid Exchange,
pubmed-meshheading:15592865-Two-Hybrid System Techniques
|
pubmed:year |
2005
|
pubmed:articleTitle |
The Drosophila melanogaster condensin subunit Cap-G interacts with the centromere-specific histone H3 variant CID.
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pubmed:affiliation |
Lehrstuhl für Genetik, University of Bayreuth, 95440 Bayreuth, Germany.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|