Evidence map›Paper›PMID 15687189›Full record

ArticleJournal of bacteriology2005

GlnD is essential for NifA activation, NtrB/NtrC-regulated gene expression, and posttranslational regulation of nitrogenase activity in the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum.

Yaoping Zhang, Edward L Pohlmann, Gary P Roberts

Abstract read
In one paragraph

Article in Journal of bacteriology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

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3 · Its place in the literature

Who cites it

25 citing papers in PubMed.

  1. Review
  2. The influence of co-encapsulatedFood chemistry: X · 2024
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  9. Genome-Wide Analyses of Proteome and Acetylome inFrontiers in microbiology · 2021
    Article
  10. Extending Viability ofFrontiers in microbiology · 2019
    Article
  11. Article
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  15. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

Yaoping ZhangDepartment of Bacteriology, University of Wisconsin--Madison, Madison, WI 53706, USA.
Edward L Pohlmann
Gary P Roberts

Funding

PII: multiple homologs of a global regulatorR01GM065891 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERTS, GARY PAUL · 2002 to 2011
$2.0M
Molecular basis of PII functionR56GM065891 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI ROBERTS, GARY PAUL · 2007 to 2007
$203k
NIGMS NIH HHS GM65891NIGMS NIH HHS R01 GM065891NIGMS NIH HHS R56 GM065891
6 · The paper itself

Abstract

GlnD is a bifunctional uridylyltransferase/uridylyl-removing enzyme and is thought to be the primary sensor of nitrogen status in the cell. It plays an important role in nitrogen assimilation and metabolism by reversibly regulating the modification of P(II) proteins, which in turn regulate a variety of other proteins. We report here the characterization of glnD mutants from the photosynthetic, nitrogen-fixing bacterium Rhodospirillum rubrum and the analysis of the roles of GlnD in the regulation of nitrogen fixation. Unlike glnD mutations in Azotobacter vinelandii and some other bacteria, glnD deletion mutations are not lethal in R. rubrum. Such mutants grew well in minimal medium with glutamate as the sole nitrogen source, although they grew slowly with ammonium as the sole nitrogen source (MN medium) and were unable to fix N(2). The slow growth in MN medium is apparently due to low glutamine synthetase activity, because a DeltaglnD strain with an altered glutamine synthetase that cannot be adenylylated can grow well in MN medium. Various mutation and complementation studies were used to show that the critical uridylyltransferase activity of GlnD is localized to the N-terminal region. Mutants with intermediate levels of uridylyltransferase activity are differentially defective in nif gene expression, the posttranslational regulation of nitrogenase, and NtrB/NtrC function, indicating the complexity of the physiological role of GlnD. These results have implications for the interpretation of results obtained with GlnD in many other organisms.

Indexed as

Gene Expression Regulation, BacterialNitrogen FixationAmmoniaBacterial ProteinsCulture MediaDNA Mutational AnalysisGene DeletionGenetic Complementation TestGlutamate SynthaseGlutamic AcidNitrogenNitrogenaseNucleotidyltransferasesPII Nitrogen Regulatory ProteinsProtein Structure, TertiaryRhodospirillum rubrumAmmoniaBacterial ProteinsCulture MediaGlutamate SynthaseGlutamic AcidNifA protein, BacteriaNitrogenNitrogenaseNucleotidyltransferasesPII Nitrogen Regulatory Proteinsregulatory protein uridylyltransferaseTranscription Factors

Identifiers

PMID15687189
PMCPMC545621

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.