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. 1996 Oct;178(20):6074–6077. doi: 10.1128/jb.178.20.6074-6077.1996

Endogenous ADP-ribosylation of proteins in Mycobacterium smegmatis.

M H Serres 1, J C Ensign 1
PMCID: PMC178471  PMID: 8830711

Abstract

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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Selected References

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