NDLI: Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii

Content Provider	PubMed Central
Author	Leonardo, Curatti Brown, Carolyn S. Ludden, Paul W. Rubio, Luis M.
Copyright Year	2005
Abstract	Rnf proteins are proposed to form membrane-protein complexes involved in the reduction of target proteins such as the transcriptional regulator SoxR or the dinitrogenase reductase component of nitrogenase. In this work, we investigate the role of rnf genes in the nitrogen-fixing bacterium Azotobacter vinelandii. We show that A. vinelandii has two clusters of rnf-like genes: rnf1, whose expression is nif-regulated, and rnf2, which is expressed independently of the nitrogen source in the medium. Deletion of each of these gene clusters produces a time delay in nitrogen-fixing capacity and, consequently, in diazotrophic growth. Δrnf mutations cause two distinguishable effects on the nitrogenase system: (i), slower nifHDK gene expression and (ii), impairment of nitrogenase function. In these mutants, dinitrogenase reductase activity is lowered, whereas dinitrogenase activity remains essentially unaltered. Further analysis indicates that Δrnf mutants accumulate an inactive and iron-deficient form of NifH because they have lower rates of incorporation of [4Fe-4S] into NifH. Δrnf mutations also cause a noticeable decrease in aconitase activity; however, they do not produce general oxidative stress or modification of Fe metabolism in A. vinelandii. Our results suggest the existence of a redox regulatory mechanism in A. vinelandii that controls the rate of expression and maturation of nitrogenase by the activity of the Rnf protein complexes. rnf1 plays a major and more specific role in this scheme, but the additive effects of mutations in rnf1 and rnf2 indicate the existence of functional complementation between the two homologous systems.
Related Links	http://dx.doi.org/10.1073/pnas.0501216102
Starting Page	6291
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	18
Volume Number	102
Language	English
Publisher	National Academy of Sciences
Publisher Date	2005-05-03
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii.

H2-uptake activity of the MoFe protein component of Azotobacter vinelandii nitrogenase.

The gene encoding dinitrogenase reductase 2 is required for expression of the second alternative nitrogenase from Azotobacter vinelandii.

Expression of the nifBfdxNnifOQ region of Azotobacter vinelandii and its role in nitrogenase activity.

Nature of Oxygen Inhibition of Nitrogenase from Azotobacter vinelandii

Two nifA-like genes required for expression of alternative nitrogenases by Azotobacter vinelandii.

Dependence of nitrogenase switch-off upon oxygen stress on the nitrogenase activity in Azotobacter vinelandii.

Electron Paramagnetic Resonance of Nitrogenase and Nitrogenase Components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP

Electron paramagnetic resonance of nitrogenase and nitrogenase components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP

Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii

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Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii.

H2-uptake activity of the MoFe protein component of Azotobacter vinelandii nitrogenase.

The gene encoding dinitrogenase reductase 2 is required for expression of the second alternative nitrogenase from Azotobacter vinelandii.

Expression of the nifBfdxNnifOQ region of Azotobacter vinelandii and its role in nitrogenase activity.

Nature of Oxygen Inhibition of Nitrogenase from Azotobacter vinelandii

Two nifA-like genes required for expression of alternative nitrogenases by Azotobacter vinelandii.

Dependence of nitrogenase switch-off upon oxygen stress on the nitrogenase activity in Azotobacter vinelandii.

Electron Paramagnetic Resonance of Nitrogenase and Nitrogenase Components from Clostridium pasteurianum W5 and Azotobacter vinelandii OP

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Genes required for rapid expression of nitrogenase activity in Azotobacter vinelandii