Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum

Fitzmaurice, Wayne P.; Saari, Leonard L.; Lowery, Robert G.; Ludden, Paul W.; Roberts, Gary P.

doi:10.1007/bf00331287

Cited by 107 publications

(89 citation statements)

References 36 publications

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“…To identify structural features necessary for activity, evolutionary conservation of sequence was investigated. Deduced amino acid sequences of the mammalian hydrolases contained only limited regions of identity to the hydrolase from R. rubrum (Table I) (20). Amino acids 60 -67, 133-139, and 285-291 of rat, mouse, and human brain hydrolase showed significant identity with bacterial ADP-ribosylarginine hydrolase.…”

Section: Resultsmentioning

confidence: 99%

“…In the photosynthetic bacterium Rhodospirillum rubrum (20), an ADP-ribosylation cycle plays an important role in nitrogen fixation, which is controlled by the reversible ADP-ribosylation of dinitrogenase reductase. An ADP-ribosyltransferase (termed DRAT for dinitrogenase reductase ADP-ribosyltransferase) inactivates dinitrogenase reductase by ADP-ribosylation, and DRAG or dinitroreductase ADP-ribosylarginine glycohydrolase regenerates the active form by releasing ADP-ribose from the enzyme (20).…”

mentioning

confidence: 99%

“…An ADP-ribosyltransferase (termed DRAT for dinitrogenase reductase ADP-ribosyltransferase) inactivates dinitrogenase reductase by ADP-ribosylation, and DRAG or dinitroreductase ADP-ribosylarginine glycohydrolase regenerates the active form by releasing ADP-ribose from the enzyme (20). This ADP-ribosylation cycle is regulated by environmental signals (e.g.…”

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confidence: 99%

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Identification of Critical, Conserved Vicinal Aspartate Residues in Mammalian and Bacterial ADP-ribosylarginine Hydrolases

Konczalik

Moss

1999

Journal of Biological Chemistry

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NAD:arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyze opposing arms of a putative ADP-ribosylation cycle. ADP-ribosylarginine hydrolases from mammalian tissues and Rhodospirillum rubrum exhibit three regions of similarity in deduced amino acid sequence. We postulated that amino acids in these consensus regions could be critical for hydrolase function. To test this hypothesis, hydrolase, cloned from rat brain, was expressed as a glutathione S-transferase fusion protein in Escherichia coli and purified by glutathione-Sepharose affinity chromatography. Conserved amino acids in each of these regions were altered by site-directed mutagenesis. Replacement of Asp-60 or Asp-61 with Ala, Gln, or Asn, but not Glu, significantly reduced enzyme activity. The double Asp-60 3 Glu/ Asp-61 3 Glu mutant was inactive, as were Asp-60 3 Gln/Asp-61 3 Gln or Asp-60 3 Asn/Asp-61 3 Asn. The catalytically inactive single and double mutants appeared to retain conformation, since they bound ADPribose, a substrate analogue and an inhibitor of enzyme activity, with affinity similar to that of the wild-type hydrolase and with the expected stoichiometry of one. Replacing His-65, Arg-139, Asp-285, which are also located in the conserved regions, with alanine did not change specific activity. These data clearly show that the conserved vicinal aspartates 60 and 61 in rat ADPribosylarginine hydrolase are critical for catalytic activity, but not for high affinity binding of the substrate analogue, ADP-ribose.

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Section: Resultsmentioning

confidence: 99%

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confidence: 99%

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Identification of Critical, Conserved Vicinal Aspartate Residues in Mammalian and Bacterial ADP-ribosylarginine Hydrolases

Konczalik

Moss

1999

Journal of Biological Chemistry

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“…The system defined by this ART adds to the diversity of potential NADutilizing protein-modifying ARTs that are analogs of the DraT-DraG system. [25][26][27]100 The newly identified BC4486-like ARTs retain the same form of the first and second catalytic motifs as KptA, while acquiring an acidic residue in the third position. This, together with the archaeo-eukaryotic origin of the ART fold, suggests that protein-modifying ARTs first emerged as a part of the bacteria-specific radiation of this fold, and the BC4486-like ARTs possibly represent an intermediate in this transition.…”

Section: Evolutionary Implications and General Conclusionmentioning

confidence: 99%

Identification of novel components of NAD-utilizing metabolic pathways and prediction of their biochemical functions

Souza

Aravind

2012

Mol. BioSyst.

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Nicotinamide adenine dinucleotide (NAD) is a ubiquitous cofactor participating in numerous redox reactions. It is also a substrate for regulatory modifications of proteins and nucleic acids via the addition of ADP-ribose moieties or removal of acyl groups by transfer to ADP-ribose. In this study, we use in-depth sequence, structure and genomic context analysis to uncover new enzymes and substrate-binding proteins in NAD-utilizing metabolic and macromolecular modification systems. We predict that Escherichia coli YbiA and related families of domains from diverse bacteria, eukaryotes, large DNA viruses and single strand RNA viruses are previously unrecognized components of NAD-utilizing pathways that probably operate on ADP-ribose derivatives. Using contextual analysis we show that some of these proteins potentially act in RNA repair, where NAD is used to remove 2 0 -3 0 cyclic phosphodiester linkages. Likewise, we predict that another family of YbiA-related enzymes is likely to comprise a novel NAD-dependent ADP-ribosylation system for proteins, in conjunction with a previously unrecognized ADP-ribosyltransferase. A similar ADP-ribosyltransferase is also coupled with MACRO or ADP-ribosylglycohydrolase domain proteins in other related systems, suggesting that all these novel systems are likely to comprise pairs of ADP-ribosylation and ribosylglycohydrolase enzymes analogous to the DraG-DraT system, and a novel group of bacterial polymorphic toxins. We present evidence that some of these coupled ADP-ribosyltransferases/ribosylglycohydrolases are likely to regulate certain restriction modification enzymes in bacteria. The ADP-ribosyltransferases found in these, the bacterial polymorphic toxin and host-directed toxin systems of bacteria such as Waddlia also throw light on the evolution of this fold and the origin of eukaryotic polyADP-ribosyltransferases and NEURL4-like ARTs, which might be involved in centrosomal assembly. We also infer a novel biosynthetic pathway that might be involved in the synthesis of a nicotinate-derived compound in conjunction with an asparagine synthetase and AMPylating peptide ligase. We use the data derived from this analysis to understand the origin and early evolutionary trajectories of key NAD-utilizing enzymes and present targets for future biochemical investigations.

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“…This list includes C3-1ike transferases [25 29], cholera toxin [30], the family of Rhodospirillum-like ADP-ribosyltransferases [31], the T2, T4, T6 bacteriophage transferases [32] and several recently identified eukaryotic glycosylphosphatidylinositol-anchored mono-ADP-ribosyltransferases (or NAD-ases) such as the rabbit muscle ADP-ribosyltransferase [33][34][35] and the family of RT6-1ike T-cell alloantigens [36][37][38].…”

Section: Resultsmentioning

confidence: 99%

Analysis of the catalytic site of the actin ADP‐ribosylating Clostridium perfringens iota toxin

Damme¹,

Jung

Hofmann

et al. 1996

FEBS Letters

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Genes coding for the reversible ADP-ribosylation system of dinitrogenase reductase from Rhodospirillum rubrum

Cited by 107 publications

References 36 publications

Identification of Critical, Conserved Vicinal Aspartate Residues in Mammalian and Bacterial ADP-ribosylarginine Hydrolases

Identification of Critical, Conserved Vicinal Aspartate Residues in Mammalian and Bacterial ADP-ribosylarginine Hydrolases

Identification of novel components of NAD-utilizing metabolic pathways and prediction of their biochemical functions

Analysis of the catalytic site of the actin ADP‐ribosylating Clostridium perfringens iota toxin

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