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J. Biol. Chem., Vol. 277, Issue 28, 24983-24987, July 12, 2002
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,,
From the Department of Chemistry, Bose Institute, 93/1 Acharya
Prafulla Chandra Road, Kolkata 700009, India
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 Asp370
of 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.
These two authors contributed equally to this work.
§
To whom correspondence should be addressed. Fax: 91-33-3506790;
E-mail: joyoti@bosemain.boseinst.ac.in.
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