Open AccessFunctional characterization of AAA family FtsH protease of Mycobacterium tuberculosis
Author(s) -
Srinivasan Ramanujam,
Anilkumar Gopalakrishnapillai,
Rajeswari Harayadi,
Ajitkumar Parthasarathi
Publication year - 2006
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.1574-6968.2006.00251.x
Subject(s) - biology , escherichia coli , mycobacterium tuberculosis , protease , protein subunit , proteolysis , heterologous , microbiology and biotechnology , proteases , mutant , metalloproteinase , biochemistry , enzyme , gene , tuberculosis , medicine , pathology
FtsH is a membrane‐bound ATP‐dependent zinc‐metalloprotease which proteolytically regulates the levels of specific membrane and cytoplasmic proteins that participate in diverse cellular functions, and which therefore might be of critical importance to a human pathogen such as Mycobacterium tuberculosis . As the substrates of MtFtsH in mycobacteria are not known, we examined whether recombinant MtFtsH could complement the lethality of a Δ ftsH 3∷kan mutation in Escherichia coli and elicit proteolytic activity against the known substrates of E. coli FtsH, namely heat shock transcription factor σ 32 protein, protein translocation subunit SecY and bacteriophage λCII repressor protein. The MtFtsH protein could not only efficiently complement lethality of Δ ftsH 3∷kan mutation in E. coli , but could also degrade all three heterologous substrates with specificity when expressed in ftsH ‐null cells of E. coli . These observations probably reveal the degree of conservation in the mechanisms of substrate recognition and cellular processes involving FtsH protease of M. tuberculosis and E. coli .