Open AccessSalicylate uniquely induces a 27‐kDa protein in tubercle bacillus
Author(s) -
Sun Zhonghe,
Cheng ShaoJi,
Zhang Hao,
Zhang Ying
Publication year - 2001
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2001.tb10843.x
Subject(s) - mycobacterium smegmatis , mycobacterium tuberculosis , biochemistry , bacillus subtilis , salicylic acid , escherichia coli , biology , microbiology and biotechnology , western blot , gene , chemistry , bacteria , tuberculosis , genetics , medicine , pathology
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.