Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis.
Endogenous ADP-ribosylation of two proteins with molecular weights of 30,000 (30K) and 80,000 (80K) was detected in cell extracts of Mycobacterium smegmatis. Modification of these proteins was enzymatic. The ADP-ribose bound to 30K was removed by HgCl2 but not by NH2OH, suggesting the modification of a cysteine residue. The ADP-ribose bound to 80K was not removed by either HgCl2 or NH2OH, which is consistent with the modification of an asparagine residue. ADP-ribosylation of 80K appeared to be reversible.
Serres
M H
MH
Department of Bacteriology, University of Wisconsin--Madison, 53706, USA.
Ensign
J C
JC
D000246:Adenosine Diphosphate Ribose / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism*; D009161:Mycobacterium / Q000378:metabolism*; D009243:NAD / Q000378:metabolism; D011065:Poly(ADP-ribose) Polymerases / Q000378:metabolism*; D011499:Protein Processing, Post-Translational
D001426:Bacterial Proteins; D009243:NAD; D000246:Adenosine Diphosphate Ribose; D011065:Poly(ADP-ribose) Polymerases