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Title: Posttranslational modification of a vanadium nitrogenase

Abstract

In microbes that fix nitrogen, nitrogenase catalyzes the conversion of N2 to ammonia in an ATP-demanding reaction. To help conserve energy some bacteria inhibit nitrogenase activity upon exposure to ammonium. The purple nonsulfur phototrophic bacterium Rhodopseudomonas palustris strain CGA009 can synthesize three functional nitrogenase isoenzymes: a molybdenum nitrogenase, a vanadium nitrogenase, and an iron nitrogenase. Previous studies showed that in some alphaproteobacteria, including R. palustris, molybdenum nitrogenase activity is inhibited by ADP-ribosylation when cells are exposed to ammonium. Some iron nitrogenases are also post-translationally modified. However, the posttranslational modification of vanadium nitrogenase has not been reported. Here, we investigated the regulation of the alternative nitrogenases of R. palustris and determined that both its vanadium nitrogenase and its iron nitrogenase activities were inhibited and post-translationally modified when cells are exposed to ammonium. Vanadium nitrogenase is not found in all strains of R. palustris, suggesting that it may have been acquired by horizontal gene transfer. Also, phylogenetic analyses of the three nitrogenases suggest that VnfH, the target of ADP-ribosylation, may be the product of a gene duplication of nifH, the molybdenum nitrogenase homolog.

Authors:
 [1];  [1]
  1. Department of Microbiology, University of Washington, Seattle Washington 98195
Publication Date:
Research Org.:
Univ. of Washington, Seattle, WA (United States)
Sponsoring Org.:
USDOE Office of Science (SC)
OSTI Identifier:
1623573
Grant/Contract Number:  
FG02-05ER15707
Resource Type:
Journal Article: Accepted Manuscript
Journal Name:
MicrobiologyOpen
Additional Journal Information:
Journal Volume: 4; Journal Issue: 4; Journal ID: ISSN 2045-8827
Publisher:
Wiley
Country of Publication:
United States
Language:
English
Subject:
Microbiology

Citation Formats

Heiniger, Erin K., and Harwood, Caroline S. Posttranslational modification of a vanadium nitrogenase. United States: N. p., 2015. Web. doi:10.1002/mbo3.265.
Heiniger, Erin K., & Harwood, Caroline S. Posttranslational modification of a vanadium nitrogenase. United States. https://doi.org/10.1002/mbo3.265
Heiniger, Erin K., and Harwood, Caroline S. 2015. "Posttranslational modification of a vanadium nitrogenase". United States. https://doi.org/10.1002/mbo3.265. https://www.osti.gov/servlets/purl/1623573.
@article{osti_1623573,
title = {Posttranslational modification of a vanadium nitrogenase},
author = {Heiniger, Erin K. and Harwood, Caroline S.},
abstractNote = {In microbes that fix nitrogen, nitrogenase catalyzes the conversion of N2 to ammonia in an ATP-demanding reaction. To help conserve energy some bacteria inhibit nitrogenase activity upon exposure to ammonium. The purple nonsulfur phototrophic bacterium Rhodopseudomonas palustris strain CGA009 can synthesize three functional nitrogenase isoenzymes: a molybdenum nitrogenase, a vanadium nitrogenase, and an iron nitrogenase. Previous studies showed that in some alphaproteobacteria, including R. palustris, molybdenum nitrogenase activity is inhibited by ADP-ribosylation when cells are exposed to ammonium. Some iron nitrogenases are also post-translationally modified. However, the posttranslational modification of vanadium nitrogenase has not been reported. Here, we investigated the regulation of the alternative nitrogenases of R. palustris and determined that both its vanadium nitrogenase and its iron nitrogenase activities were inhibited and post-translationally modified when cells are exposed to ammonium. Vanadium nitrogenase is not found in all strains of R. palustris, suggesting that it may have been acquired by horizontal gene transfer. Also, phylogenetic analyses of the three nitrogenases suggest that VnfH, the target of ADP-ribosylation, may be the product of a gene duplication of nifH, the molybdenum nitrogenase homolog.},
doi = {10.1002/mbo3.265},
url = {https://www.osti.gov/biblio/1623573}, journal = {MicrobiologyOpen},
issn = {2045-8827},
number = 4,
volume = 4,
place = {United States},
year = {Fri Jun 19 00:00:00 EDT 2015},
month = {Fri Jun 19 00:00:00 EDT 2015}
}

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