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Please use this identifier to cite or link to this item: http://dspace.library.iitb.ac.in/jspui/handle/10054/4619

Title: Glutamate-induced assembly of bacterial cell division protein FtsZ
Authors: BEURIA, TK
KRISHNAKUMAR, SS
SAHAR, S
SINGH, N
GUPTA, K
MESHRAM, M
PANDA, D
Keywords: microtubule-associated proteins
escherichia-coli
dynamic instability
binding-protein
gtp hydrolysis
brain tubulin
polymerization
ring
homolog
mechanism
Issue Date: 2003
Publisher: AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation: JOURNAL OF BIOLOGICAL CHEMISTRY, 278(6), 3735-3741
Abstract: The polymerization of FtsZ is a finely regulated process that plays an essential role in the bacterial cell division process. However, only a few modulators of FtsZ polymerization are known. We identified monosodium glutamate as a potent inducer of FtsZ polymerization. In the presence of GTP, glutamate enhanced the rate and extent of polymerization of FtsZ in a concentration-dependent manner; similar to90% of the protein was sedimented as polymer in the presence of 1 m glutamate. Electron micrographs of glutamate-induced polymers showed large filamentous structures with extensive bundling. Furthermore, glutamate strongly stabilized the polymers against dilution-induced disassembly, and it decreased the GTPase activity of FtsZ. Calcium induced FtsZ polymerization and bundling of FtsZ polymers; interestingly, although 1 m glutamate produced a larger light-scattering signal than produced by 10 mm calcium, the amount of polymer sedimented in the presence of 1 m glutamate and 10 mm calcium was similar. Thus, the increased light scattering in the presence of glutamate must be due to its ability to induce more extensive bundling of FtsZ polymers than calcium. The data suggest that calcium and glutamate might induce FtsZ polymerization by different mechanisms.
URI: http://dx.doi.org/10.1074/jbc.M205760200
http://dspace.library.iitb.ac.in/xmlui/handle/10054/4619
http://hdl.handle.net/10054/4619
ISSN: 0021-9258
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