Functional relationship between Escherichia coli RNase E and the CafA protein

Mol Gen Genet. 1997 Jan 27;253(4):515-9. doi: 10.1007/s004380050352.

Abstract

We analyzed the functional relationship between the Escherichia coli RNase E and the CafA protein, which show extensive sequence similarity. The temperature-sensitive growth of the RNase E mutant strain ams1 was partially suppressed by multicopy plasmids bearing the cafA gene. Introduction of a cafA::cat mutation enhanced the temperature sensitivity of the ams1 mutant. These results suggest that there is a functional homology between these two proteins.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacterial Proteins / physiology*
  • Endoribonucleases / chemistry
  • Endoribonucleases / genetics
  • Endoribonucleases / physiology*
  • Escherichia coli / enzymology
  • Escherichia coli / genetics
  • Escherichia coli / growth & development
  • Escherichia coli / physiology*
  • Escherichia coli Proteins*
  • Genes, Bacterial
  • Mutagenesis, Insertional
  • Temperature

Substances

  • Bacterial Proteins
  • Escherichia coli Proteins
  • Endoribonucleases
  • rng protein, E coli
  • ribonuclease E