ArticleJournal of bacteriology2001
Functional characterization of three GlnB homologs in the photosynthetic bacterium Rhodospirillum rubrum: roles in sensing ammonium and energy status.
Article in Journal of bacteriology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed.
- A singular PpaA/AerR-like protein inmSystems · 2023Article
- Potential of Phototrophic Purple Nonsulfur Bacteria to Fix Nitrogen in Rice Fields.Microorganisms · 2021Review
- Interaction between Nitrogen and Phosphate Stress Responses inFrontiers in microbiology · 2016Article
- Effect of point mutations on Herbaspirillum seropedicae NifA activity.Brazilian journal of medical and biological research = Revista brasileira de pesquisas medicas e biologica · 2015Article
- Article
- P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- The nitrogenase regulatory enzyme dinitrogenase reductase ADP-ribosyltransferase (DraT) is activated by direct interaction with the signal transduction protein GlnB.Journal of bacteriology · 2013Article
- Molecular basis for the distinct divalent cation requirement in the uridylylation of the signal transduction proteins GlnJ and GlnB from Rhodospirillum rubrum.BMC microbiology · 2012Article
- How posttranslational modification of nitrogenase is circumvented in Rhodopseudomonas palustris strains that produce hydrogen gas constitutively.Applied and environmental microbiology · 2012Article
- Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The poor growth of Rhodospirillum rubrum mutants lacking RubisCO is due to the accumulation of ribulose-1,5-bisphosphate.Journal of bacteriology · 2011Article
- Structure of GlnK1, a signalling protein from Archaeoglobus fulgidus.Acta crystallographica. Section F, Structural biology and crystallization communications · 2011Article
- Elimination of Rubisco alters the regulation of nitrogenase activity and increases hydrogen production in Rhodospirillum rubrum.International journal of hydrogen energy · 2010Article
- Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein.Journal of bacteriology · 2010Article
- GlnB/GlnK PII proteins and regulation of the Sinorhizobium meliloti Rm1021 nitrogen stress response and symbiotic function.Journal of bacteriology · 2010Article
- Nitrogenase switch-off and regulation of ammonium assimilation in response to light deprivation in Rhodospirillum rubrum are influenced by the nitrogen source used during growth.Journal of bacteriology · 2010Article
- Effect of perturbation of ATP level on the activity and regulation of nitrogenase in Rhodospirillum rubrum.Journal of bacteriology · 2009Article
- A mutant GlnD nitrogen sensor protein leads to a nitrogen-fixing but ineffective Sinorhizobium meliloti symbiosis with alfalfa.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Identification and functional characterization of NifA variants that are independent of GlnB activation in the photosynthetic bacterium Rhodospirillum rubrum.Microbiology (Reading, England) · 2008Article
- Specificity and regulation of interaction between the PII and AmtB1 proteins in Rhodospirillum rubrum.Journal of bacteriology · 2007Article
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4 authors.
Funding
Abstract
The GlnB (P(II)) protein, the product of glnB, has been characterized previously in the photosynthetic bacterium Rhodospirillum rubrum. Here we describe identification of two other P(II) homologs in this organism, GlnK and GlnJ. Although the sequences of these three homologs are very similar, the molecules have both distinct and overlapping functions in the cell. While GlnB is required for activation of NifA activity in R. rubrum, GlnK and GlnJ do not appear to be involved in this process. In contrast, either GlnB or GlnJ can serve as a critical element in regulation of the reversible ADP ribosylation of dinitrogenase reductase catalyzed by the dinitrogenase reductase ADP-ribosyl transferase (DRAT)/dinitrogenase reductase-activating glycohydrolase (DRAG) regulatory system. Similarly, either GlnB or GlnJ is necessary for normal growth on a variety of minimal and rich media, and any of the proteins is sufficient for normal posttranslational regulation of glutamine synthetase. Surprisingly, in their regulation of the DRAT/DRAG system, GlnB and GlnJ appeared to be responsive not only to changes in nitrogen status but also to changes in energy status, revealing a new role for this family of regulators in central metabolic regulation.
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