Salicylate uniquely induces a 27-kDa protein in tubercle bacillus

Zhonghe Sun, Shao Ji Cheng, Hao Zhang, Ying Zhang

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16 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)211-216
Number of pages6
JournalFEMS microbiology letters
Issue number2
StatePublished - Sep 25 2001


  • Induction
  • Mycobacterium tuberculosis
  • Protein
  • Salicylate

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics


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