A cold-active heat-labile t-RNA modification GTPase from a psychrophilic bacterium Pseudomonas syringae (Lz4W)

Res Microbiol. 2010 Jan-Feb;161(1):46-50. doi: 10.1016/j.resmic.2009.11.002. Epub 2009 Nov 24.

Abstract

A cold-active heat-labile t-RNA modification GTPase (TrmE) from psychrophilic bacterium Pseudomonas syringae (Lz4W) has been purified and characterized. The purified TrmE is a 53 kDa protein, has GTPase activity and hydrolyses only the oxy and deoxy forms of GTP but not the other nucleotide triphosphates. The enzyme exhibits optimal activity at 12-18 degrees C and retains 65% of its optimal activity at 4 degrees C, indicating that it is a cold-active enzyme. The enzyme is also heat-labile and loses 60% of its activity at 30 degrees C. This is the first report on the purification and characterization of a TrmE from a psychrophilic bacterium.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cold Temperature
  • Enzyme Stability
  • GTP Phosphohydrolases / chemistry
  • GTP Phosphohydrolases / isolation & purification*
  • GTP Phosphohydrolases / metabolism*
  • Guanosine Triphosphate / metabolism*
  • Hot Temperature
  • Molecular Weight
  • Pseudomonas syringae / enzymology*
  • RNA, Transfer / metabolism*
  • Substrate Specificity
  • Time Factors

Substances

  • Guanosine Triphosphate
  • RNA, Transfer
  • GTP Phosphohydrolases