Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Adenosine Triphosphatases / metabolism*
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Animals
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Centromere / chemistry
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Centromere / metabolism*
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Centromere Protein A
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Chromosome Segregation
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DNA-Binding Proteins / metabolism*
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Drosophila Proteins / metabolism*
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Drosophila melanogaster / genetics
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Drosophila melanogaster / metabolism*
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Embryo, Nonmammalian / cytology
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Embryo, Nonmammalian / drug effects
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Embryo, Nonmammalian / metabolism
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Female
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Histones / genetics
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Histones / metabolism*
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Kinetochores / metabolism
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Male
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Microfilament Proteins / metabolism
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Mitosis
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Multiprotein Complexes
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Mutation / genetics
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Protein Binding
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Protein Subunits
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Saccharomyces cerevisiae / genetics
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Sister Chromatid Exchange
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Two-Hybrid System Techniques
Substances
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Centromere Protein A
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Cid protein, Drosophila
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DNA-Binding Proteins
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Drosophila Proteins
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Histones
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Microfilament Proteins
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Multiprotein Complexes
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Protein Subunits
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condensin complexes
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Adenosine Triphosphatases