RNA polymerase II degradation in response to rapamycin is not mediated through ubiquitylation

Biochem Biophys Res Commun. 2011 Sep 23;413(2):248-53. doi: 10.1016/j.bbrc.2011.08.079. Epub 2011 Aug 23.

Abstract

In Saccharomyces cerevisiae, the immunosuppressor rapamycin engenders the degradation of excessive RNA polymerase II leading to growth arrest but the regulation of this process is not known yet. Here, we show that this mechanism is dependent on the peptidyl prolyl cis/trans isomerase Rrd1. Strikingly this degradation is independent of RNA polymerase II polyubiquitylation and does not require the elongation factor Elc1. Our data reveal that there are at least two alternative pathways to degrade RNA polymerase II that depend on different type of stresses.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Immunosuppressive Agents / pharmacology*
  • Intracellular Signaling Peptides and Proteins / genetics
  • Intracellular Signaling Peptides and Proteins / metabolism*
  • Peptidylprolyl Isomerase / genetics
  • Peptidylprolyl Isomerase / metabolism*
  • RNA Polymerase II / metabolism*
  • Saccharomyces cerevisiae / drug effects*
  • Saccharomyces cerevisiae / enzymology
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Sirolimus / pharmacology*
  • Ubiquitination

Substances

  • Immunosuppressive Agents
  • Intracellular Signaling Peptides and Proteins
  • Saccharomyces cerevisiae Proteins
  • RNA Polymerase II
  • Peptidylprolyl Isomerase
  • RRD1 protein, S cerevisiae
  • Sirolimus