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J. Bacteriol., Oct 1996, 6074-6077, Vol 178, No. 20
Copyright © 1996, American Society for Microbiology

Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis

MH Serres and JC Ensign
Department of Bacteriology, University of Wisconsin--Madison, 53706, USA.

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.


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