Abstract
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 language | English (US) |
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Pages (from-to) | 211-216 |
Number of pages | 6 |
Journal | FEMS microbiology letters |
Volume | 203 |
Issue number | 2 |
DOIs | |
State | Published - Sep 25 2001 |
Keywords
- Induction
- Mycobacterium tuberculosis
- Protein
- Salicylate
ASJC Scopus subject areas
- Microbiology
- Molecular Biology
- Genetics