HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

J. Biol. Chem., Vol. 278, Issue 6, 3735-3741, February 7, 2003

This Article Full Text Full Text (PDF) All Versions of this Article: 278/6/3735    most recent M205760200v1 Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Beuria, T. K. Articles by Panda, D. Search for Related Content PubMed PubMed Citation Articles by Beuria, T. K. Articles by Panda, D. Social Bookmarking                      What's this?

Glutamate-induced Assembly of Bacterial Cell Division Protein FtsZ^*

Tushar K. Beuria, Shyam Sundar Krishnakumar, Saurabh Sahar, Neera Singh, Kamlesh Gupta, Mallika Meshram, and Dulal Panda^§

From the School of Biosciences and Bioengineering, Indian Institute of Technology, Bombay, Powai, Mumbai 400 076, India

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; ~90% 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.

CiteULike

Complore

Connotea

Del.icio.us

Digg

Reddit

Technorati

This article has been cited by other articles:

				R. Diaz-Espinoza, A. P. Garces, J. J. Arbildua, F. Montecinos, J. E. Brunet, R. Lagos, and O. Monasterio Domain folding and flexibility of Escherichia coli FtsZ determined by tryptophan site-directed mutagenesis Protein Sci., August 1, 2007; 16(8): 1543 - 1556. [Abstract] [Full Text] [PDF]

				B. D. Corbin, Y. Wang, T. K. Beuria, and W. Margolin Interaction between Cell Division Proteins FtsE and FtsZ J. Bacteriol., April 15, 2007; 189(8): 3026 - 3035. [Abstract] [Full Text] [PDF]

				J. M. Gonzalez, M. Velez, M. Jimenez, C. Alfonso, P. Schuck, J. Mingorance, M. Vicente, A. P. Minton, and G. Rivas Cooperative behavior of Escherichia coli cell-division protein FtsZ assembly involves the preferential cyclization of long single-stranded fibrils PNAS, February 8, 2005; 102(6): 1895 - 1900. [Abstract] [Full Text] [PDF]

				R. Marrington, E. Small, A. Rodger, T. R. Dafforn, and S. G. Addinall FtsZ Fiber Bundling Is Triggered by a Conformational Change in Bound GTP J. Biol. Chem., November 19, 2004; 279(47): 48821 - 48829. [Abstract] [Full Text] [PDF]

				M. K. Santra, T. K. Beuria, A. Banerjee, and D. Panda Ruthenium Red-induced Bundling of Bacterial Cell Division Protein, FtsZ J. Biol. Chem., June 18, 2004; 279(25): 25959 - 25965. [Abstract] [Full Text] [PDF]

				S. P. Anand, H. Rajeswari, P. Gupta, R. Srinivasan, S. Indi, and P. Ajitkumar A C-terminal deletion mutant of Mycobacterium tuberculosis FtsZ shows fast polymerization in vitro Microbiology, May 1, 2004; 150(5): 1119 - 1121. [Full Text] [PDF]