Modification of proteins by mono(ADP-ribosylation) in vivo

Dm, Payne; El, Jacobson; Moss, Joel; Mk, Jacobson

doi:10.1021/bi00347a006

Cited by 63 publications

(36 citation statements)

References 35 publications

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“…8A) and Rt6 -2 (Fig. 8B) were incubated under conditions known to cleave specifically the linkage of ADPR to thiol groups (10 mM HgCl 2 ) or to arginine (1 M neutral NH 2 OH) (47,48). The M2L-bound label is resistant to overnight treatment with PBS (lanes 1), 10 mM NAD ϩ (lanes 2), 1 M NaCl (lanes 3), and 10 mM HgCl 2 (lane 5), but sensitive to treatment with 1 M NH 2 OH (lane 4).…”

Section: Recombinant Rt6 -1 and Rt6 -2 Bound To M2 Sepharose Beads Camentioning

confidence: 99%

Mouse T Cell Membrane Proteins Rt6−1 and Rt6−2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins

Koch-Nolte

Petersen

Balasubramanian

et al. 1996

Journal of Biological Chemistry

122

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Mono ADP-ribosylation is a posttranslational protein modification that has been implicated in the regulation of key biological functions in bacteria as well as in animals. Recently, the first cDNAs for eucaryotic mono-(ADPribosyl)transferases were cloned and found to exhibit significant sequence similarity only to one other known protein, the T cell differentiation antigen Rt6. In this paper we describe secondary structure analyses of Rt6 and related proteins and show conserved structure motifs and amino acid residues consistent with a common ancestry of these eucaryotic proteins and bacterial ADP-ribosyltransferases. Moreover, we have expressed soluble mouse Rt6 -1 and Rt6 -2 gene products in which C-terminal tags (FLAG-His 6 ) replace the native glycosylphosphatidylinositol anchor signal sequences. Purified recombinant Rt6 -2, but not Rt6 -1, shows NAD ؉ glycohydrolase activity, which is inhibited by the arginine analogue agmatine. Immunoprecipitation of recombinant Rt6 -1 and Rt6 -2 with anti-FLAG M2 antibody followed by incubation with [ P]NAD؉ leads to rapid and covalent incorporation of radioactivity into the light chain of the M2 antibody. The bound label is resistant to treatment with HgCl 2 but sensitive to NH 2 OH, characteristic of arginine-linked ADP-ribosylation. These results demonstrate that Rt6 -1 and Rt6 -2 possess the enzymatic activities typical for NAD ؉ -dependent arginine/ protein mono(ADPribosyl)transferases (EC 2.4.2.31). They are the first such enzymes to be molecularly characterized in the immune system.

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Section: Recombinant Rt6 -1 and Rt6 -2 Bound To M2 Sepharose Beads Camentioning

confidence: 99%

Mouse T Cell Membrane Proteins Rt6−1 and Rt6−2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins

Koch-Nolte

Petersen

Balasubramanian

et al. 1996

Journal of Biological Chemistry

122

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“…The complete cleavage of NAD+ was controlled using SAX-HPLC-chromatography, following the method described by Payne et al [36].…”

Section: Synthesis Of (32p]adp-rihosementioning

confidence: 99%

Characterization of a nitric‐oxide‐catalysed ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase

Dimmeler

Brüne

1992

European Journal of Biochemistry

128

102

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Auto-ADP-ribosylation of the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase (GraPDH) has recently been demonstrated to be dramatically stimulated in the presence of nitric oxide. In order to obtain insight into the sequence of events leading to ADP-ribosylation of GraPDH, we studied the target amino acid, the nucleotide cofactor requirement, pH dependency and the stoichiometry of the reaction. Basal as well as stimulated ADP-ribose transfer is inhibited by the SH-group alkylating reagent, N-ethylmaleimide. Furthermore, the radiolabel of a~t o -[~~P ] A D pribosylated GraPDH is removed by treatment with HgC12, suggesting an ADP-ribose -cysteine bond. Several indirect and direct mechanistic considerations point to NAD' as the only cofactor for the ADP-ribosylation reaction, excluding the possibility of a reaction sequence involving a NADglycohydrolase(s) followed by nonenzymatic ADP-ribose transfer to GraPDH. Optimal ADPribosylations were carried out at alkaline pH values using 10 pM free NAD' as the sole nucleotide cofactor. Bovine serum albumin with an S-nitrosylated SH group can serve as a model of ADP-ribose transfer from NAD' and suggests that the nitric-oxide-modified SH group (S-nitrosylated SH group) is a prerequisite for the reaction. In a previous work, we demonstrated that nitric oxide was able to increase the mono-ADP-ribosylation of a 39-kDa cytosolic protein [18, 191, which was observed not only when nitric oxide was released from pharmacological compounds like sodium nitroprusside (SNP) or 3-morpholino-sydnonimine (SIN-l), but also when nitric oxide was generated from its physiological precursor L-arginine, by the enzymic activity of the nitric oxide synthase [22]. Nitric-oxide-stimulated ADP-ribosylation was recently confirmed by two other groups, using cerebral cortex and erythrocyte membranes [21, 231. These studies may suggest that endogenous ADP-ribosylation is under the regulatory control of second messenger systems, especially nitric oxide. Activation of nitric oxide synthase [24] in its various isoforms [25] produces nitric oxide, initially characterized as the endothelium-derived relaxing factor [26]. While some nitric oxide effects are mediated by binding of nitric oxide to the heme subunit of soluble guanylate cyclase, thus increasing cGMP [27], the stimulatory effects concerning the mono-ADPribosylation are cGMP independent and might be linked to higher and hence pathophysiological and cytotoxic nitric oxide conditions [28, 291. Our studies now further characterize this nitric-oxidecatalysed mono-ADP-ribosylation of GraPDH and explore some mechanistics of the ADP-ribose-transfer reaction. We would like to stress the importance of reduced thiol groups as a prerequisite for ADP-ribosylation, furthermore we would like to report on cysteine-specific modification, pH dependency and the specificity of NAD+, required for this ADPribosylation reaction.

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“…The different ADP-ribose-protein linkages have different sensitivities to hydroxylamine [28]. The ADP-ribose-glutamate and other carboxylate ester bonds are extremely labile to hydroxylamine.…”

Section: Resultsmentioning

confidence: 99%

“…[28] and Meyer et al [29]. Samples were prelabelled and washed as described for the snake venom phosphodiesterase experiments.…”

Section: Snake Venom Phosphodiesterase Digestion Of Adp-ribosylated Smentioning

confidence: 99%

Localization and partial characterization of ADP-ribosylation products in hearts from adult and neonatal rats

Piron

McMahon

1990

Biochemical Journal

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The subcellular distributions of endogenous ADP-ribosylation products in hearts from 1-day-old neonatal and adult rats were investigated. In adult rat heart a 52 kDa mono-ADP-ribosylation product was identified in the plasma membrane fraction. In contrast, in neonatal rat heart a 130 kDa poly-ADP-ribosylation product was present in the nuclear fraction. The monomeric and polymeric nature of the two ADP-ribosylation products was determined by their sensitivity to thymidine and by analysis of their snake venom phosphodiesterase products. NADP+ enhanced both the mono-and polymeric reactions. The ADP-ribose-protein linkage of the adult 52 kDa product was stable to 1 h of treatment with hydroxylamine (0.5 M) and mercury ions, but was sensitive to alkali and a 12 h treatment with hydroxylamine (1 M). This is suggestive of an arginine linkage. The 130 kDa poly-ADP-ribosylation product from the neonatal rat heart was alkalilabile but stable to both hydroxylamine and HgCl2. This implies the presence of an unusual linkage in the 130 kDa product. The presence of these different ADP-ribosylation products in adult and neonatal rat hearts suggests the possible importance of these proteins and their ADP-ribosylation during cardiac development.

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Modification of proteins by mono(ADP-ribosylation) in vivo

Cited by 63 publications

References 35 publications

Mouse T Cell Membrane Proteins Rt6−1 and Rt6−2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins

Mouse T Cell Membrane Proteins Rt6−1 and Rt6−2 Are Arginine/Protein Mono(ADPribosyl)transferases and Share Secondary Structure Motifs with ADP-ribosylating Bacterial Toxins

Characterization of a nitric‐oxide‐catalysed ADP‐ribosylation of glyceraldehyde‐3‐phosphate dehydrogenase

Localization and partial characterization of ADP-ribosylation products in hearts from adult and neonatal rats

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