ArticleThe Journal of biological chemistry2009
In vitro interactions between the PII proteins and the nitrogenase regulatory enzymes dinitrogenase reductase ADP-ribosyltransferase (DraT) and dinitrogenase reductase-activating glycohydrolase (DraG) in Azospirillum brasilense.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Ethylene signals through an ethylene receptor to modulate biofilm formation and root colonization in a beneficial plant-associated bacterium.PLoS genetics · 2025Article
- Article
- The Role of Nitric Oxide in Nitrogen Fixation by Legumes.Frontiers in plant science · 2020Review
- 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
- 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
- Tools for genetic manipulation of the plant growth-promoting bacterium Azospirillum amazonense.BMC microbiology · 2011Article
- Role of PII proteins in nitrogen fixation control of Herbaspirillum seropedicae strain SmR1.BMC microbiology · 2011Article
- 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
- Characterization of the DraT/DraG system for posttranslational regulation of nitrogenase in the endophytic betaproteobacterium Azoarcus sp. strain BH72.Journal of bacteriology · 2009Article
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7 authors.
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Abstract
The activity of the nitrogenase enzyme in the diazotroph Azospirillum brasilense is reversibly inactivated by ammonium through ADP-ribosylation of the nitrogenase NifH subunit. This process is catalyzed by DraT and is reversed by DraG, and the activities of both enzymes are regulated according to the levels of ammonium through direct interactions with the P(II) proteins GlnB and GlnZ. We have previously shown that DraG interacts with GlnZ both in vivo and in vitro and that DraT interacts with GlnB in vivo. We have now characterized the influence of P(II) uridylylation status and the P(II) effectors (ATP, ADP, and 2-oxoglutarate) on the in vitro formation of DraT-GlnB and DraG-GlnZ complexes. We observed that both interactions are maximized when P(II) proteins are de-uridylylated and when ADP is present. The DraT-GlnB complex formed in vivo was purified to homogeneity in the presence of ADP. The stoichiometry of the DraT-GlnB complex was determined by three independent approaches, all of which indicated a 1:1 stoichiometry (DraT monomer:GlnB trimer). Our results suggest that the intracellular fluctuation of the P(II) ligands ATP, ADP, and 2-oxoglutarate play a key role in the post-translational regulation of nitrogenase activity.
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