Protein phosphorylation is involved in the regulation of chromatin condensation during interphase

Viktor Dombrádi, Paricia T.W. Cohen

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

Loci affecting the condensation state of interphase chromatin have been previously identified from analysis of suppression and enhancement of position effect variegation (PEV) in Drosophila. Here we show that Su-var(3)6 and an allelic mutant, e078, which both show suppression of PEV in the heterozygous state, have point mutations (Gly220→Ser and Gly220→Asp, respectively) in a protein phosphatase 1 catalytic subunit located at 87B (PP1 87B). The mutated glycine is conserved in all known protein serine/threonine phosphatases in the same gene family, and its substitution decreases PP1 activity. We conclude that protein dephosphorylation by PP1 87B regulates the condensation state of chromatin during interphase.

Original languageEnglish
Pages (from-to)21-26
Number of pages6
JournalFEBS letters
Volume312
Issue number1
DOIs
Publication statusPublished - Nov 2 1992

    Fingerprint

Keywords

  • Chromatin
  • Drosophila
  • Mitosis
  • Position effect variegation
  • Protein phosphatase

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

Cite this