Abstract
In Rhodospirillum rubrum, nitrogenase activity is subject to posttranslational regulation through the adenosine diphosphate (ADP)-ribosylation of dinitrogenase reductase by dinitrogenase reductase ADP-ribosyltransferase (DRAT) and dinitrogenase reductase-activating glycohydrolase (DRAG). To study the posttranslational regulation of DRAG, its gene was mutagenized and colonies screened for altered DRAG regulation. Three different mutants were found and the DRAG variants displayed different biochemical properties including an altered affinity for divalent metal ions. Taken together, the results suggest that the site involved in regulation is physically near the metal binding site of DRAG.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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ADP Ribose Transferases / genetics
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ADP Ribose Transferases / metabolism*
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Adenosine Diphosphate Ribose / metabolism
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Binding Sites
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Cations, Divalent / metabolism
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Dinitrogenase Reductase / metabolism
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Mutagenesis
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Mutation
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N-Glycosyl Hydrolases / genetics
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N-Glycosyl Hydrolases / metabolism*
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Protein Processing, Post-Translational / genetics*
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Rhodospirillum rubrum / enzymology*
Substances
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Cations, Divalent
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Dinitrogenase Reductase
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Adenosine Diphosphate Ribose
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ADP Ribose Transferases
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dinitrogenase reductase ADP-ribosyltransferase
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N-Glycosyl Hydrolases
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ADP-ribosyl-(dinitrogen reductase) hydrolase