ArticleJournal of bacteriology2007
In vitro studies of the uridylylation of the three PII protein paralogs from Rhodospirillum rubrum: the transferase activity of R. rubrum GlnD is regulated by alpha-ketoglutarate and divalent cations but not by glutamine.
Article in Journal of bacteriology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 25 citations in OpenAlex.
- Microaerobic dark fermentation by purple bacteria as an emerging perspective for biohydrogen production-a review.Biotechnology for biofuels and bioproducts · 2026Review
- 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
- Mechanism of 2-oxoglutarate signaling by the Synechococcus elongatus PII signal transduction protein.Proceedings of the National Academy of Sciences of the United States of America · 2010Article
- Mutagenesis and functional characterization of the four domains of GlnD, a bifunctional nitrogen sensor protein.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
- Mechanism of ADP-ribosylation removal revealed by the structure and ligand complexes of the dimanganese mono-ADP-ribosylhydrolase DraG.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- 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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2 authors at 1 institution in 1 country.
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Abstract
P(II) proteins have been shown to be key players in the regulation of nitrogen fixation and ammonia assimilation in bacteria. The mode by which these proteins act as signals is by being in either a form modified by UMP or the unmodified form. The modification, as well as demodification, is catalyzed by a bifunctional enzyme encoded by the glnD gene. The regulation of this enzyme is thus of central importance. In Rhodospirillum rubrum, three P(II) paralogs have been identified. In this study, we have used purified GlnD and P(II) proteins from R. rubrum, and we show that for the uridylylation activity of R. rubrum GlnD, alpha-ketoglutarate is the main signal, whereas glutamine has no effect. This is in contrast to, e.g., the Escherichia coli system. Furthermore, we show that all three P(II) proteins are uridylylated, although the efficiency is dependent on the cation present. This difference may be of importance in understanding the effects of the P(II) proteins on the different target enzymes. Furthermore, we show that the deuridylylation reaction is greatly stimulated by glutamine and that Mn(2+) is required.
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