Open AccessEndogenous ADP-ribosylation of proteins in Mycobacterium smegmatis
Author(s) -
Mireille Serres,
Jerald C. Ensign
Publication year - 1996
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.178.20.6074-6077.1996
Subject(s) - mycobacterium smegmatis , biology , adp ribosylation , cysteine , endogeny , asparagine , biochemistry , residue (chemistry) , enzyme , microbiology and biotechnology , mycobacterium tuberculosis , medicine , tuberculosis , nad+ kinase , pathology
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.