Functional implications of the conserved action of regulators of ribonuclease activity

J Microbiol Biotechnol. 2008 Aug;18(8):1353-6.


RNase E (Rne) plays a major role in the decay and processing of numerous RNAs in E. coli, and protein inhibitors of RNase E, RraA and RraB, have recently been discovered. Here, we report that coexpression of RraA or RraB reduces the ribonucleolytic activity in rne-deleted E. coli cells overproducing RNase ES, a Streptomyces coelicolor functional ortholog of RNase E, and consequently rescues these cells from growth arrest. These findings suggest that the regulators of ribonuclease activity have a conserved intrinsic property that effectively acts on an RNase E-like enzyme found in a distantly related bacterial species.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Endoribonucleases / antagonists & inhibitors
  • Endoribonucleases / deficiency
  • Endoribonucleases / metabolism*
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Escherichia coli Proteins / biosynthesis*
  • Escherichia coli Proteins / genetics
  • Gene Expression Regulation, Bacterial*
  • RNA, Bacterial / genetics
  • RNA, Bacterial / metabolism
  • Reverse Transcriptase Polymerase Chain Reaction


  • Escherichia coli Proteins
  • RNA, Bacterial
  • RraA protein, E coli
  • RraB protein, E coli
  • Endoribonucleases
  • ribonuclease E