Mycobacterial RNase E-associated proteins

Microbiol Immunol. 2005;49(11):1003-7. doi: 10.1111/j.1348-0421.2005.tb03697.x.

Abstract

RNase E and its complex with other proteins ('degradosome') play an important role in RNA processing and decay in Escherichia coli and in many other bacteria. To identify the proteins which can potentially interact with this enzyme in mycobacteria, Mycobacterium tuberculosis H37Rv RNase E was cloned and expressed as a 6HisFLAG-tagged fusion protein. Analysis of the mycobacterial RNase E overexpressed and purified from M. bovis BCG revealed the presence of GroEL and two other copurified proteins, products of the Mb1721 (inorganic polyphosphate/ATP-NAD kinase) and Mb0825c (acetyltransferase) genes. Identical copies of these two genes can be found in M. tuberculosis H37Rv.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Endoribonucleases / metabolism
  • Endoribonucleases / physiology*
  • Escherichia coli / genetics*
  • Escherichia coli / metabolism*
  • Multienzyme Complexes / physiology*
  • Mycobacterium / genetics*
  • Mycobacterium / metabolism
  • Polyribonucleotide Nucleotidyltransferase / physiology*
  • RNA Helicases / physiology*

Substances

  • Multienzyme Complexes
  • degradosome
  • Polyribonucleotide Nucleotidyltransferase
  • Endoribonucleases
  • ribonuclease E
  • RNA Helicases