Statements in which the resource exists as a subject.
PredicateObject
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.
pubmed:affiliation
Lehrstuhl für Genetik, University of Bayreuth, 95440 Bayreuth, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't