Amino acid-specific ADP-ribosylation.
作者： J Moss , D A Yost , S J Stanley
DOI: 10.1016/S0021-9258(18)32434-7
关键词:
摘要: [adenine-U-14C]ADP-ribose-agmatine and [adenine-U-14C ))ADP-ribose-histone were synthesized by an NAD:arginine ADP-ribosyltransferase from [14C]NAD agmatine histone, respectively. The pseudo-first order rate constants for breakdown of the two components either in 0.4 N NaOH or M neutral hydroxylamine identical. Hydroxylamine treatment [14C]ADP-ribose-agmatine [32P]ADP-ribose-histone yielded a single radioactive product which was separated high pressure liquid chromatography identified as ADP-ribose-hydroxamate formation ferric chloride complex. Hydrolysis with snake venom phosphodiesterase resulted 5'-AMP, consistent presence pyrophosphate bond. Incubation ADP-ribose-[14C]agmatine, NAD [14C]agmatine, release [14C]agmatine rather than phosphoribosyl[14C]agmatine. In addition, neither nor ADP-ribose reacts hydroxylamine; i.e. there no evidence nucleophilic attack at ADP-ribosyl-protein linkage formed is considerably more stable to ADP-ribose-glutamate ADP-ribose-arginine poly(ADP-ribose) synthetase, respectively, may be chemical basis "hydroxylamine-stable" "hydroxylamine-labile" bonds described Hilz (Hilz, H. (1981) Hoppe-Seyler's Z. Physiol. Chem. 362, 1415-1425).
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