Consequences of RNase E scarcity in Escherichia coli

Mol Microbiol. 2002 Feb;43(4):1053-64. doi: 10.1046/j.1365-2958.2002.02808.x.


The endoribonuclease RNase E plays an important role in RNA processing and degradation in Escherichia coli. The construction of an E. coli strain in which the cellular concentration of RNase E can be precisely controlled has made it possible to examine and quantify the effect of RNase E scarcity on RNA decay, gene regulation and cell growth. These studies show that RNase E participates in a step in the degradation of its RNA substrates that is partially or fully rate-determining. Our data also indicate that E. coli growth requires a cellular RNase E concentration at least 10-20% of normal and that the feedback mechanism that limits overproduction of RNase E is also able to increase its synthesis when its concentration drops below normal. The magnitude of the in-crease in RNA longevity under conditions of RNase E scarcity may be limited by an alternative pathway for RNA degradation. Additional experiments show that RNase E is a stable protein in E. coli. No other E. coli gene product, when either mutated or cloned on a multicopy plasmid, seems to be capable of compensating for an inadequate supply of this essential protein.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Cell Division
  • Endoribonucleases / genetics
  • Endoribonucleases / metabolism*
  • Enzyme Stability
  • Escherichia coli / drug effects
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Gene Expression Regulation, Bacterial
  • Gene Expression Regulation, Enzymologic
  • Genes, Bacterial
  • Homeostasis
  • Isopropyl Thiogalactoside / pharmacology
  • RNA, Bacterial / metabolism
  • RNA, Messenger / metabolism
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism


  • RNA, Bacterial
  • RNA, Messenger
  • Recombinant Fusion Proteins
  • Isopropyl Thiogalactoside
  • Endoribonucleases
  • ribonuclease E