Open AccessADP‐ribosylation of membrane proteins of Streptomyces griseus strain 52‐1
Author(s) -
Penyige András,
Barabás György,
Szabó István,
Ensign C.
Publication year - 1990
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1990.tb04247.x
Subject(s) - streptomyces griseus , biochemistry , enzyme , guanidine , nad+ kinase , streptomyces albus , oligomycin , adp ribosylation , arginine , biology , streptomyces , chemistry , bacteria , amino acid , atpase , genetics
Membranes purified from cells of Streptomyces griseus strain 52‐1 possess and ADP‐ribosyltransferase acrivity. The enzyme transfers the DP‐ribose moiety of NAD to one major membrane protein of M r 32000 and 2–3 minot 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.