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

Chromosoma. 2005 Feb;113(7):350-61. doi: 10.1007/s00412-004-0322-4. Epub 2004 Dec 9.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphatases / metabolism*
  • Animals
  • Centromere / chemistry
  • Centromere / metabolism*
  • Centromere Protein A
  • Chromosome Segregation
  • DNA-Binding Proteins / metabolism*
  • Drosophila Proteins / metabolism*
  • Drosophila melanogaster / genetics
  • Drosophila melanogaster / metabolism*
  • Embryo, Nonmammalian / cytology
  • Embryo, Nonmammalian / drug effects
  • Embryo, Nonmammalian / metabolism
  • Female
  • Histones / genetics
  • Histones / metabolism*
  • Kinetochores / metabolism
  • Male
  • Microfilament Proteins / metabolism
  • Mitosis
  • Multiprotein Complexes
  • Mutation / genetics
  • Protein Binding
  • Protein Subunits
  • Saccharomyces cerevisiae / genetics
  • Sister Chromatid Exchange
  • Two-Hybrid System Techniques

Substances

  • Centromere Protein A
  • Cid protein, Drosophila
  • DNA-Binding Proteins
  • Drosophila Proteins
  • Histones
  • Microfilament Proteins
  • Multiprotein Complexes
  • Protein Subunits
  • condensin complexes
  • Adenosine Triphosphatases