{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["284(11)"],"submitter":["Huergo LF"],"funding":["Biotechnology and Biological Sciences Research Council"],"pubmed_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 A"],"journal":["The Journal of biological chemistry"],"pagination":["6674-82"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2652340"],"repository":["biostudies-literature"],"pubmed_title":["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."],"pmcid":["PMC2652340"],"pubmed_authors":["Chubatsu LS","Steffens MB","Pedrosa FO","Merrick M","Souza EM","Monteiro RA","Huergo LF"],"additional_accession":[]},"is_claimable":false,"name":"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.","description":"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 A","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Mar","modification":"2025-04-20T02:08:44.886Z","creation":"2019-03-27T00:21:05Z"},"accession":"S-EPMC2652340","cross_references":{"pubmed":["19131333"],"doi":["10.1074/jbc.M807378200","10.1074/jbc.m807378200"]}}