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P(II) signal transduction proteins: nitrogen regulation and beyond.
The P(II) proteins are one of the most widely distributed families of signal transduction proteins in nature. They are pivotal players in the control of nitrogen metabolism in bacteria and archaea,Expand
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ADP‐ribosylation of dinitrogenase reductase in Azospirillum brasilense is regulated by AmtB‐dependent membrane sequestration of DraG
Nitrogen fixation in some diazotrophic bacteria is regulated by mono‐ADP‐ribosylation of dinitrogenase reductase (NifH) that occurs in response to addition of ammonium to the extracellular medium.Expand
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A new P(II) protein structure identifies the 2-oxoglutarate binding site.
P(II) proteins of bacteria, archaea, and plants regulate many facets of nitrogen metabolism. They do so by interacting with their target proteins, which can be enzymes, transcription factors, orExpand
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Interaction of the Nitrogen Regulatory Protein GlnB (PII) with Biotin Carboxyl Carrier Protein (BCCP) Controls Acetyl-CoA Levels in the Cyanobacterium Synechocystis sp. PCC 6803
The family of PII signal transduction proteins (members GlnB, GlnK, NifI) plays key roles in various cellular processes related to nitrogen metabolism at different functional levels. Recent studiesExpand
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The Emergence of 2-Oxoglutarate as a Master Regulator Metabolite
  • L. Huergo, R. Dixon
  • Biology, Medicine
  • Microbiology and Molecular Reviews
  • 30 September 2015
SUMMARY The metabolite 2-oxoglutarate (also known as α-ketoglutarate, 2-ketoglutaric acid, or oxoglutaric acid) lies at the intersection between the carbon and nitrogen metabolic pathways. ThisExpand
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Ternary complex formation between AmtB, GlnZ and the nitrogenase regulatory enzyme DraG reveals a novel facet of nitrogen regulation in bacteria
Ammonium movement across biological membranes is facilitated by a class of ubiquitous channel proteins from the Amt/Rh family. Amt proteins have also been implicated in cellular responses to ammoniumExpand
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PII signal transduction proteins: pivotal players in post-translational control of nitrogenase activity.
The fixation of atmospheric nitrogen by the prokaryotic enzyme nitrogenase is an energy- expensive process and consequently it is tightly regulated at a variety of levels. In many diazotrophs thisExpand
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Campylobacter jejuni Dps protein binds DNA in the presence of iron or hydrogen peroxide.
Iron is an essential cofactor for many enzymes; however, this metal can lead to the formation of reactive oxygen species. Ferritin proteins bind and oxidize Fe(2+) to Fe(3+), storing this metal in aExpand
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Crystal structure of the GlnZ-DraG complex reveals a different form of PII-target interaction
Nitrogen metabolism in bacteria and archaea is regulated by a ubiquitous class of proteins belonging to the PIIfamily. PII proteins act as sensors of cellular nitrogen, carbon, and energy levels, andExpand
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In Vitro Interactions between the PII Proteins and the Nitrogenase Regulatory Enzymes Dinitrogenase Reductase ADP-ribosyltransferase (DraT) and Dinitrogenase Reductase-activating Glycohydrolase
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 isExpand
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