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FEMS Microbiol Lett. 1990 Jun 1;57(3):293-7.

ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1.

Author information

1
Institute of Biology, University Medical School, Debrecen, Hungary.

Abstract

Membranes purified from cells of Streptomyces griseus strain 52-1 possess an ADP-ribosyltransferase activity. The enzyme transfers the ADP-ribose moiety of NAD to one major membrane protein of Mr 32,000 and 2-3 minor proteins of larger molecular weights. The effects of inhibitors on the ADP-ribosyltransferase activity proves that the reaction is enzymatic and suggests that the enzyme ADP-ribosylates the guanidine group of arginine. The kinetics of liberation of ADP-ribose during alkaline hydrolysis of the modified proteins is consistent with the arginine-ADP-ribose bond. This is the first report of ADP-ribosylation of proteins in a Gram-positive bacterium.

PMID:
2120108
DOI:
10.1016/0378-1097(90)90083-3
[Indexed for MEDLINE]

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