Salicylate uniquely induces a 27-kDa protein in tubercle bacillus.
Salicylate was found to uniquely induce a 27-kDa protein in Mycobacterium tuberculosis complex organisms but not in Mycobacterium smegmatis or Escherichia coli. The structural analogue antitubercular para-amino-salicylate also induced the 27-kDa protein but to a somewhat lower level than salicylate. Other structural analogues such as benzoic acid and acetyl salicylic acid (aspirin) did not induce the 27-kDa protein. Western blot analysis indicated that the 27-kDa protein was localized mainly in the cytoplasm. The 27-kDa protein was not expressed at different growth phases in the absence of salicylate. The 27-kDa protein was identified as a putative benzoquinone methyltransferase (Rv0560c), which has several homologues in the M. tuberculosis genome. The cloned 27-kDa gene was found to express constitutively in E. coli, M. smegmatis and BCG with or without salicylate.
Sun
Z
Z
Department of Molecular Microbiology and Immunology, School of Hygiene and Public Health, Johns Hopkins University, 615 N. Wolfe Street, Baltimore, MD 21205, USA.
Cheng
S J
SJ
Zhang
H
H
Zhang
Y
Y
D010131:Aminosalicylic Acid / Q000494:pharmacology; D001426:Bacterial Proteins / Q000096:biosynthesis* / Q000235:genetics; D016227:Benzoquinones / Q000378:metabolism; D003470:Culture Media; D004790:Enzyme Induction; D008780:Methyltransferases / Q000096:biosynthesis* / Q000235:genetics; D009169:Mycobacterium tuberculosis / Q000187:drug effects* / Q000201:enzymology* / Q000254:growth & development; D012459:Salicylates / Q000494:pharmacology*
D001426:Bacterial Proteins; D016227:Benzoquinones; D003470:Culture Media; D012459:Salicylates; C004532:quinone; D010131:Aminosalicylic Acid; D008780:Methyltransferases