ASURA (PHB2) interacts with Scc1 through chromatin

Cytogenet Genome Res. 2013;139(4):225-33. doi: 10.1159/000350004. Epub 2013 Mar 23.

Abstract

Sister chromatid cohesion mediated by the cohesin complex is essential for faithful chromosome segregation. Previously we reported that PHB2 (prohibitin2/ASURA), a multifunctional protein, has a role in sister chromatid cohesion. Nevertheless, how ASURA is involved in sister chromatid cohesion still remains unclear. The present co-immunoprecipitation analysis reveals that ASURA interacts with cohesin subunit Scc1 in vivo. We show that ASURA associates with chromatin in a similar manner as Scc1 throughout the cell cycle. Furthermore, our observation using the Fucci (fluorescent ubiquitination-based cell cycle indicator) system indicates that ASURA is important for cohesin maintenance at early mitosis. We have also identified that the conserved PHB domain is responsible for chromatin targeting of ASURA. Our results suggest that the regulation of sister chromatid cohesion is mediated by ASURA binding to chromatin, where ASURA might be involved in cohesin protection through ASURA-Scc1 interactions.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Count
  • Cell Cycle Proteins / genetics
  • Cell Cycle Proteins / metabolism*
  • Cell Nucleus / genetics
  • Cell Nucleus / metabolism
  • Centromere / genetics
  • Centromere / metabolism
  • Chromatids / genetics
  • Chromatids / metabolism
  • Chromatin / genetics
  • Chromatin / metabolism*
  • Chromatin Assembly and Disassembly
  • Chromosomal Proteins, Non-Histone / genetics
  • Chromosomal Proteins, Non-Histone / metabolism*
  • DNA-Binding Proteins
  • Fluorescent Dyes / metabolism
  • G2 Phase Cell Cycle Checkpoints
  • HeLa Cells
  • Humans
  • Mitochondria / genetics
  • Mitochondria / metabolism
  • Mitosis
  • Nuclear Proteins / genetics
  • Nuclear Proteins / metabolism*
  • Phosphoproteins / genetics
  • Phosphoproteins / metabolism*
  • Protein Binding
  • Protein Interaction Mapping / methods*
  • Protein Structure, Tertiary
  • RNA Interference
  • Repressor Proteins / genetics
  • Repressor Proteins / metabolism*

Substances

  • Cell Cycle Proteins
  • Chromatin
  • Chromosomal Proteins, Non-Histone
  • DNA-Binding Proteins
  • Fluorescent Dyes
  • Nuclear Proteins
  • Phosphoproteins
  • RAD21 protein, human
  • Repressor Proteins
  • cohesins
  • prohibitin