Ubiquitin-specific peptidase 42 (USP42) functions to deubiquitylate histones and regulate transcriptional activity

J Biol Chem. 2014 Dec 12;289(50):34862-70. doi: 10.1074/jbc.M114.589267. Epub 2014 Oct 21.

Abstract

Ubiquitin-specific peptidase 42 (USP42) is a deubiquitylating enzyme that can target p53 and contribute to the stabilization of p53 in response to stress. We now show that USP42 can also regulate transcription independently of p53. USP42 co-localized with RNA polymerase II (RNA Pol II) in nuclear foci, bound to histone H2B, and deubiquitylated H2B. Depletion of USP42 increased H2B ubiquitylation at a model promoter and decreased both basal and induced transcription from a number of promoters. These results are consistent with a role for USP42 in regulating transcription by deubiquitylating histones.

Keywords: Chromatin; Deubiquitylation (Deubiquitination); Histone; RNA Polymerase II; Transcription; USP42.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Active Transport, Cell Nucleus
  • Cell Line
  • Cell Nucleus / metabolism
  • Cyclin-Dependent Kinase Inhibitor p21 / genetics
  • Gene Expression Regulation*
  • Gene Knockdown Techniques
  • Histones / metabolism*
  • Humans
  • Promoter Regions, Genetic / genetics
  • Thiolester Hydrolases / deficiency
  • Thiolester Hydrolases / genetics
  • Thiolester Hydrolases / metabolism*
  • Transcription, Genetic*
  • Ubiquitination*

Substances

  • Cyclin-Dependent Kinase Inhibitor p21
  • Histones
  • USP42 protein, human
  • Thiolester Hydrolases