Characterization of altered regulation variants of dinitrogenase reductase-activating glycohydrolase from Rhodospirillum rubrum

• Published in: FEBS letters Vol. 559; no. 1; pp. 84 - 88
• Main Authors: Kim, Kitai, Zhang, Yaoping, Roberts, Gary P
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 13.02.2004
• Subjects: Adenosine Diphosphate Ribose - metabolism; Adenosine diphosphate-ribosylation; ADP Ribose Transferases - genetics; ADP Ribose Transferases - metabolism; Binding Sites; Cations, Divalent - metabolism; Dinitrogenase Reductase - metabolism; Dinitrogenase reductase-activating glycohydrolase; Mutagenesis; Mutation; N-Glycosyl Hydrolases - genetics; N-Glycosyl Hydrolases - metabolism; Nitrogen fixation; Posttranslational regulation; Protein Processing, Post-Translational - genetics; Rhodospirillum rubrum; Rhodospirillum rubrum - enzymology; Nitrogen fixation; Adenosine diphosphate-ribosylation; Rhodospirillum rubrum; Dinitrogenase reductase-activating glycohydrolase; Posttranslational regulation
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(04)00031-6

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.