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. 1985 Sep;82(17):5603–5607. doi: 10.1073/pnas.82.17.5603

Reversibility of arginine-specific mono(ADP-ribosyl)ation: identification in erythrocytes of an ADP-ribose-L-arginine cleavage enzyme.

J Moss, M K Jacobson, S J Stanley
PMCID: PMC390599  PMID: 2994036

Abstract

Enzymes have been identified in animal tissues that catalyze the mono(ADP-ribosyl)ation of arginine and proteins. Since these NAD:arginine ADP-ribosyltransferases under physiological conditions do not appear to catalyze the degradation of the product ADP-ribose-arginine, the possibility was investigated that a different family of enzymes exists that cleaves the ADP-ribose-arginine linkage. An enzyme was identified in and partially purified from turkey erythrocytes that catalyzed the degradation of ADP-ribose-[14C]arginine synthesized by a salt-activated NAD:arginine ADP-ribosyl-transferase, resulting in the release of a radiolabeled compound that was characterized chromatographically and by amino acid analysis as arginine. This putative arginine product was converted in a reaction dependent on NAD and the NAD:arginine ADP-ribosyltransferase to a compound exhibiting properties characteristic of ADP-ribose-arginine. Action of cleavage enzyme on [adenine-U-14C]ADP-ribose-arginine resulted in the release of a radiolabeled compound that behaved chromatographically like [adenine-U-14C]ADP-ribose. Since degradation of ADP-ribose-arginine appears to generate an arginine moiety that is a substrate for the NAD:arginine ADP-ribosyltransferase, it appears that ADP-ribosylation may be a reversible modification of proteins.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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