Document Detail


Regulation of Nitrogenase by Reversible Mono-ADP-Ribosylation.
MedLine Citation:
PMID:  24934999     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Posttranslational modification of proteins plays a key role in the regulation of a plethora of metabolic functions. Protein modification by mono-ADP-ribosylationmono-ADP-ribosylation was first described as a mechanism of action of bacterial toxins. Since these pioneering studies, the number of pathways regulated by ADP-ribosylation in organisms from all domains of life expanded significantly. However, in only a few cases the full regulatory ADP-ribosylation circuit is known. Here, we review the system where mono-ADP-ribosylation regulates the activity of an enzyme: the regulation of nitrogenasenitrogenase in bacteria. When the nitrogenase product, ammonium, becomes available, the ADP-ribosyltransferase (DraT) covalently links an ADP-ribose moiety to a specific arginine residue on nitrogenase switching-off nitrogenase activity. After ammonium exhaustion, the ADP-ribosylhydrolase (DraG) removes the modifying group, restoring nitrogenase activity. DraT and DraG activities are reversibly regulated through interaction with PII signaling proteinsPII signaling proteins . Bioinformatics analysis showed that DraTDraT homologs are restricted to a few nitrogen-fixing bacteria while DraG homologs are widespread in Nature. Structural comparisons indicated that bacterial DraGDraG is closely related to Archaea and mammalian ADP-ribosylhydrolases (ARH). In all available structures, the ARH active site consists of a hydrophilic cleft carrying a binuclear Mg(2+) or Mn(2+) cluster, which is critical for catalysis.
Authors:
Vivian R Moure; Flavia F Costa; Leonardo M Cruz; Fabio O Pedrosa; Emanuel M Souza; Xiao-Dan Li; Fritz Winkler; Luciano F Huergo
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2014-6-17
Journal Detail:
Title:  Current topics in microbiology and immunology     Volume:  -     ISSN:  0070-217X     ISO Abbreviation:  Curr. Top. Microbiol. Immunol.     Publication Date:  2014 Jun 
Date Detail:
Created Date:  2014-6-17     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0110513     Medline TA:  Curr Top Microbiol Immunol     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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