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    Interaction between FtsZ and FtsW of mycobacterium tuberculosis

    Datta, P. and Dasgupta, A. and Bhakta, Sanjib and Basu, J. (2002) Interaction between FtsZ and FtsW of mycobacterium tuberculosis. Journal of Biological Chemistry 277 (28), pp. 24983-24987. ISSN 0021-9258.

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    Abstract

    The recruitment of FtsZ to the septum and its subsequent interaction with other cell division proteins in a spatially and temporally controlled manner are the keys to bacterial cell division. In the present study, we have tested the hypothesis that FtsZ and FtsW of Mycobacterium tuberculosis could be binding partners. Using gel renaturation, pull-down, and solid-phase assays, we confirm that FtsZ and FtsW interact through their C-terminal tails, which carry extensions absent in their Escherichia coli counterparts. Crucial to these interactions is the cluster of aspartate residues Asp367 to Asp370of FtsZ, which most likely interact with a cluster of positively charged residues in the C-terminal tail of FtsW. Mutations of the aspartate residues 367–370 showed that changing three aspartate residues to alanine resulted in complete loss of interaction. This is the first demonstration of the direct interaction between FtsZ and FtsW. We speculate that this interaction between FtsZ and FtsW could serve to anchor FtsZ to the membrane and link septum formation to peptidoglycan synthesis in M. tuberculosis. The findings assume particular significance in view of the global efforts to explore new targets in M. tuberculosis for chemotherapeutic intervention.

    Metadata

    Item Type: Article
    School: Birkbeck Schools and Departments > School of Science > Biological Sciences
    Depositing User: Sarah Hall
    Date Deposited: 30 Apr 2019 14:53
    Last Modified: 30 Jul 2019 22:16
    URI: http://eprints.bbk.ac.uk/id/eprint/27369

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