Dinitrogenase reductase-activating glycohydrolase can be released from chromatophores of Rhodospirillum rubrum by treatment with MgGDP

J Bacteriol. 1997 Dec;179(24):7872-4. doi: 10.1128/jb.179.24.7872-7874.1997.

Abstract

Dinitrogenase reductase-activating glycohydrolase (DRAG), involved in the regulation of nitrogenase activity in Rhodospirillum rubrum, is associated with chromatophore membranes in cell extracts. We show that DRAG can be specifically released by treatment with MgGDP; other nucleotides studied had no effect. The DRAG activity released corresponds to the release of DRAG protein.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Enzyme Activation
  • Gene Expression Regulation, Bacterial
  • Glycoside Hydrolases / metabolism*
  • Guanosine Diphosphate / pharmacology*
  • Intracellular Membranes / drug effects*
  • N-Glycosyl Hydrolases*
  • Nitrogen Fixation
  • Nitrogenase / drug effects
  • Nucleotides / pharmacology
  • Photosynthetic Reaction Center Complex Proteins / drug effects*
  • Rhodospirillum rubrum / enzymology*

Substances

  • Nucleotides
  • Photosynthetic Reaction Center Complex Proteins
  • Guanosine Diphosphate
  • Nitrogenase
  • Glycoside Hydrolases
  • N-Glycosyl Hydrolases
  • ADP-ribosyl-(dinitrogen reductase) hydrolase