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Functional characterization of AAA family FtsH protease of Mycobacterium tuberculosis

Srinivasan, Ramanujam and Anilkumar, Gopalakrishnapillai and Rajeswari, Haraydi and Ajitkumar, Parthasarathi (2006) Functional characterization of AAA family FtsH protease of Mycobacterium tuberculosis. In: FEMS Microbiology Letters, 259 (1). pp. 97-105.

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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 $\DeltaftsH3\:\:kan$ mutation in Escherichia coli and elicit proteolytic activity against the known substrates of E. coli FtsH, namely heat shock transcription factor $\sigma^3^2$ protein, protein translocation subunit SecY and bacteriophage ${\lambda}CII$ repressor protein. The MtFtsH protein could not only efficiently complement lethality of $\DeltaftsH3\:\:kan$ 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.

Item Type: Journal Article
Publication: FEMS Microbiology Letters
Publisher: Blackwell
Additional Information: Copyright of this article belongs to Blackwell.
Department/Centre: Division of Biological Sciences > Microbiology & Cell Biology
Date Deposited: 13 Feb 2007
Last Modified: 19 Sep 2010 04:27
URI: http://eprints.iisc.ac.in/id/eprint/7108

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