Reversible ADP-ribosylation as a mechanism of enzyme regulation in procaryotes

Mol Cell Biochem. 1994 Sep;138(1-2):123-9. doi: 10.1007/BF00928453.

Abstract

Several cases of ADP-ribosylation of endogenous proteins in procaryotes have been discovered and investigated. The most thoroughly studied example is the reversible ADP-ribosylation of the dinitrogenase reductase from the photosynthetic bacterium Rhodospirillum rubrum and related bacteria. A dinitrogenase reductase ADP-ribosyltransferase (DRAT) and a dinitrogenase reductase ADP-ribose glycohydrolase (DRAG) from R. rubrum have been isolated and characterized. The genes for these proteins have been isolated and sequences and show little similarity to the ADP-ribosylating toxins. Other targets for endogenous ADP-ribosylation by procaryotes include glutamine synthetase in R. rubrum and Rhizobium meliloti and undefined proteins in Streptomyces griseus and Pseudomonas maltophila.

Publication types

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

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism*
  • Bacteria / enzymology*
  • Glutamate-Ammonia Ligase / metabolism
  • Nitrogenase / metabolism

Substances

  • Adenosine Diphosphate Ribose
  • Nitrogenase
  • Glutamate-Ammonia Ligase