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• W2067453597 abstract "Posttranslational regulation of nitrogenase, or switch-off, in the methanogenic archaeon Methanococcus maripaludis requires both nifI 1 and nifI 2 , which encode members of the PII family of nitrogen-regulatory proteins. Previous work demonstrated that nitrogenase activity in cell extracts was inhibited in the presence of NifI 1 and NifI 2 , and that 2-oxoglutarate (2OG), a potential signal of nitrogen limitation, relieved this inhibition. To further explore the role of the NifI proteins in switch-off, we found proteins that interact with NifI 1 and NifI 2 and determined whether 2OG affected these interactions. Anaerobic purification of His-tagged NifI 2 resulted in copurification of NifI 1 and the dinitrogenase subunits NifD and NifK, and 2OG or a deletion mutation affecting the T-loop of NifI 2 prevented copurification of dinitrogenase but did not affect copurification of NifI 1 . Similar results were obtained with His-tagged NifI 1 . Gel-filtration chromatography demonstrated an interaction between purified NifI 1,2 and dinitrogenase that was inhibited by 2OG. The NifI proteins themselves formed a complex of ≈85 kDa, which appeared to further oligomerize in the presence of 2OG. NifI 1,2 inhibited activity of purified nitrogenase when present in a 1:1 molar ratio to dinitrogenase, and 2OG fully relieved this inhibition. These results suggest a model for switch-off of nitrogenase activity, where direct interaction of a NifI 1,2 complex with dinitrogenase causes inhibition, which is relieved by 2OG. The presence of nifI 1 and nifI 2 in the nif operons of all nitrogen-fixing Archaea and some anaerobic Bacteria suggests that this mode of nitrogenase regulation may operate in a wide variety of diazotrophs." @default.
• W2067453597 created "2016-06-24" @default.
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• W2067453597 date "2006-06-27" @default.
• W2067453597 modified "2023-09-27" @default.
• W2067453597 title "Regulation of nitrogenase by 2-oxoglutarate-reversible, direct binding of a PII-like nitrogen sensor protein to dinitrogenase" @default.
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• W2067453597 doi "https://doi.org/10.1073/pnas.0602278103" @default.
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