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Papers In Press, published online ahead of print May 6, 2002
Chemistry, Bose Institute, Calcutta, West Bengal 700 009
Corresponding Author: joyoti{at}bosemain.boseinst.ac.in
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-tails which carry extensions absent in their E. coli counterparts. Crucial to these interactions is the cluster of aspartate residues D367 to D370 of FtsZ which most likely interact with a cluster of positively charged residues in the C-tail of FtsW. Mutations of the aspartate residues 367 to 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.
J. Biol. Chem, 10.1074/jbc.M203847200
Submitted on April 22, 2002
Revised on May 3, 2002
Accepted on May 5, 2002
Interaction between FtsZ and FtsW of mycobacterium tuberculosis
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