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Posttranslational modification of a vanadium nitrogenase.

Erin K Heiniger1, Caroline S Harwood1

  • 1Department of Microbiology, University of Washington, Seattle, Washington, 98195.

Microbiologyopen
|June 23, 2015
PubMed
Summary
This summary is machine-generated.

Rhodopseudomonas palustris regulates nitrogenase activity by inhibiting vanadium and iron nitrogenases upon ammonium exposure. These alternative nitrogenases undergo posttranslational modification, suggesting a conserved energy-saving mechanism.

Keywords:
Hydrogen productionRhodopseudomonas palustrisnitrogen fixation

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Area of Science:

  • Microbiology
  • Biochemistry
  • Molecular Biology

Background:

  • Nitrogenase catalyzes nitrogen fixation in microbes.
  • Some bacteria regulate nitrogenase activity to conserve energy.
  • Rhodopseudomonas palustris has three nitrogenase isoenzymes: molybdenum, vanadium, and iron.

Purpose of the Study:

  • Investigate the regulation of alternative nitrogenases (vanadium and iron) in R. palustris.
  • Determine if vanadium and iron nitrogenases are posttranslationally modified.
  • Explore the evolutionary origins of vanadium nitrogenase.

Main Methods:

  • Exposure of R. palustris to ammonium.
  • Analysis of nitrogenase activity.
  • Investigation of posttranslational modifications.
  • Phylogenetic analysis of nitrogenase genes.

Main Results:

  • Vanadium and iron nitrogenase activities were inhibited upon ammonium exposure.
  • Both vanadium and iron nitrogenases were posttranslationally modified.
  • Vanadium nitrogenase may have been acquired via horizontal gene transfer.
  • Phylogenetic analysis suggests VnfH originated from a duplication of nifH.

Conclusions:

  • R. palustris regulates vanadium and iron nitrogenases via posttranslational modification in response to ammonium.
  • This regulation is an energy-saving mechanism.
  • The VnfH protein may be a result of gene duplication, indicating evolutionary adaptation.