Inactivation of glutamine synthetases by an NAD:arginine ADP-ribosyltransferase.

Moss, Joel; Watkins, Paul A.; Stanley, S J; Purnell, Michael R.; Kidwell, William R.

doi:10.1016/s0021-9258(17)42962-0

Cited by 33 publications

(4 citation statements)

References 25 publications

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“…1988). This finding is in agreement with the reported specificity of transferase A for arginine side chains (Yost & Moss, 1983;Moss et al, 1980Moss et al, , 1984Moss et al, , 1985Moss et al, , 1990. It seems that transferase A rather unspecifically catalyzes ADP-ribosylation because of the various substrate proteins.…”

Section: Discussionsupporting

confidence: 90%

“…Turkey erythrocyte ADP-ribosyltransferase type A modifies several proteins, such as glutamine synthetase (Moss et al, 1984), tubulin (Scaife et al. 1992), microtubule-associated proteins (Scaife et al, 1992), and skeletal muscle a-actin.…”

Section: Discussionmentioning

confidence: 99%

“…Transferase A modifies simple guanidino compounds, like agmatine, a simple arginine derivative, which is also a cholera toxin substrate (Moss et al, 1985) but not a substrate for actin-ADP-ribosylating toxins. Glutamine synthetases from ovine brain (Moss et al, 1984) and from Escherichia coli (Moss et al, 1990) are ADP-ribosylated by transferase A, a modification inhibiting synthetase activity (Moss et al, 1984(Moss et al, , 1990).…”

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confidence: 99%

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ADP-Ribosyltransferase Type A from Turkey Erythrocytes Modifies Actin at Arg-95 and Arg-372

Just

Sehr²,

Jung³

et al. 1995

Biochemistry

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Turkey erythrocyte ADP-ribosyltransferase A catalyzes the transfer of ADP-ribose from NAD to both monomeric and polymeric skeletal muscle alpha-actin with the incorporation of 2 mol of ADP-ribose per mol of actin. In contrast, Clostridium perfringens iota toxin ADP-ribosylates only G-actin, with modification at arginine-177 [Vandekerckhove, J., et al. (1987) FEBS Lett. 255, 48-42]. Transferase A-catalyzed modifications are sensitive to 0.5 M neutral hydroxylamine, consistent with the arginine side chain modification. Radiolabeled peptides ADP-ribosylated by transferase A were generated by tryptic digestion and purified by reversed phase high-performance liquid chromatography. Amino acid sequence and molecular mass analysis identified the ADP-ribosylation sites as Arg-95 and Arg-372 of actin; both residues are located within subdomain-1 of the actin 3D structure [Kabsch, W., et al. (1990) Nature 347, 37-44]. ADP-ribosylation did not affect cytochalasin D-stimulated G-actin ATPase, the binding of actin to DNase I or to gelsolin, or the ability of actin to polymerize. Following ADP-ribosylation, however, a prolonged delay in polymerization was observed, consistent with a decreased rate of nucleation.

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Section: Discussionsupporting

confidence: 90%

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

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ADP-Ribosyltransferase Type A from Turkey Erythrocytes Modifies Actin at Arg-95 and Arg-372

Just

Sehr²,

Jung³

et al. 1995

Biochemistry

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“…NAD:arginine ADP-ribosyltransferases have been noted to catalyze the ADP-ribosylation of many proteins, presumably due to the presence of a readily accessible arginine (Moss et al, 1984;Moss & Vaughan, 1978). On the basis of studies with glutamine synthetase, it would appear that certain arginine residues are more susceptible to ADP-ribosylation and that, in some cases, these arginines may play a critical role in function (Moss et al, 1984). Presumably in the cell, the amounts of ADP-ribosylated proteins then reflect a balance between transferase, hydrolase, and the availability of acceptor.…”

Section: Discussionmentioning

confidence: 99%

Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes

Moss¹,

Tsai²,

Adamik³

et al. 1988

Biochemistry

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ADP-ribosylation of arginine appears to be a reversible modification of proteins with NAD: arginine ADP-ribosyltransferases and ADP-ribosylarginine hydrolases catalyzing the opposing arms of the ADP-ribosylation cycle. ADP-ribosylarginine hydrolases have been purified extensively (greater than 90%) (150,000-250,000-fold) from the soluble fraction of turkey erythrocytes by DE-52, phenyl-Sepharose, hydroxylapatite, Ultrogel AcA 54, and Mono Q chromatography. Mobilities of the hydrolase on gel permeation columns and on sodium dodecyl sulfate-polyacrylamide gel electrophoresis under reducing conditions are consistent with an active monomeric species of approximately 39 kDa. Insertion of an organomercurial agarose chromatographic step prior to Ultrogel AcA 54 resulted in the isolation of a hydrolase exhibiting approximately 35-fold greater sensitivity to dithiothreitol (Ka,sensitive = 41 +/- 16.7 microM, n = 4; Ka,resistant = 1.44 +/- 0.12 mM, n = 3). A similar dithiothreitol-sensitive hydrolase was generated by exposure of the purified resistant enzyme to HgCl2. At 30 degrees C, both thiol-sensitive (HS) and thiol-resistant (HR) hydrolases were relatively resistant to N-ethylmaleimide (NEM); incubation with dithiothreitol prior to NEM resulted in complete inactivation. Both HS and HR required Mg2+ and thiol for enzymatic activity. Mg2+ stabilized both HS and HR against thermal inactivation in the absence and presence of thiol. A purified NAD:arginine ADP-ribosyltransferase, in the presence of NAD, inactivated both HS and HR; Mg2+ and to a greater extent Mg2+ plus dithiothreitol protected both HS and HR from NAD- and transferase-dependent inactivation. Thus, activation of the hydrolase enhanced its resistance to inactivation by transferase.(ABSTRACT TRUNCATED AT 250 WORDS)

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Structure and function of eukaryotic mono-ADP-ribosyltransferases

Okazaki

Moss

1996

Reviews of Physiology Biochemistry and Pharmacology, Volume 129

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Inactivation of glutamine synthetases by an NAD:arginine ADP-ribosyltransferase.

Cited by 33 publications

References 25 publications

ADP-Ribosyltransferase Type A from Turkey Erythrocytes Modifies Actin at Arg-95 and Arg-372

ADP-Ribosyltransferase Type A from Turkey Erythrocytes Modifies Actin at Arg-95 and Arg-372

Purification and characterization of ADP-ribosylarginine hydrolase from turkey erythrocytes

Structure and function of eukaryotic mono-ADP-ribosyltransferases

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