ADP-ribosylation of membrane proteins of Streptomyces griseus strain 52-1.
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.
Penyige
A
A
Institute of Biology, University Medical School, Debrecen, Hungary.
Barabás
G
G
Szabó
I
I
Ensign
J C
JC
D001426:Bacterial Proteins / Q000378:metabolism; D002851:Chromatography, High Pressure Liquid; D002855:Chromatography, Thin Layer; D007700:Kinetics; D008565:Membrane Proteins / Q000378:metabolism*; D008970:Molecular Weight; D009243:NAD / Q000378:metabolism; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D013305:Streptomyces griseus / Q000201:enzymology / Q000378:metabolism*
D001426:Bacterial Proteins; D008565:Membrane Proteins; D000067856:Poly(ADP-ribose) Polymerase Inhibitors; D009243:NAD; D011065:Poly(ADP-ribose) Polymerases