The Drosophila melanogaster condensin subunit Cap-G interacts with the centromere-specific histone H3 variant CID

被引:37
作者
Jäger, H
Rauch, M
Heidmann, S
机构
[1] Univ Bayreuth, Lehrstuhl Genet, D-95440 Bayreuth, Germany
[2] Astra Zeneca Ltd, D-22880 Wedel, Germany
关键词
D O I
10.1007/s00412-004-0322-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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.
引用
收藏
页码:350 / 361
页数:12
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