Abstract
ESCHERICHIA COLI divides by forming a septum across the middle of the cell. The biochemical mechanism underlying this process is unknown. Genetic evidence suggests that of all the fts (filamentation temperature sensitive) genes1,2 involved in E. coli cell division, ftsZ plays a central role at the earliest known step of septation3–5. Here we show that FtsZ protein binds GTP in vitro using unusual sequence elements6–8. In contrast, such binding to the product of the conditional-lethal ftsZ84 allele is impaired. Purified FtsZ displays a Mg2+-dependent GTPase activity which is markedly reduced in the FtsZ84 protein. FtsZ copurifies with near stoichiometric amounts of noncovalently-bound GDP, implying the presence of a GTPase cycle in vivo, similar to that known for signal-transducing GTP-binding proteins8,9. We also show that a small fraction of FtsZ exists as a distinct membrane-associated species that binds GTP. The membrane association of FtsZ and the known ability of GTPases to act as molecular switches8,9 implicate FtsZ in a GTP-activated signal transduction pathway that may regulate the start of septation in E. coli.
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References
Donachie, W. D., Begg, K. J. & Sullivan, N. F. in Microbial Development (ed. Losick, R. & Shapiro, L.) 27–62 (Cold Spring Harbor Laboratory, New York, 1984).
de Boer, P. A. J., Cook, W. R., & Rothfield, L. I. A. Rev. Genet. 24, 249–274 (1990).
Lutkenhaus, J. Trends Genet. 6, 22–25 (1990).
Begg, K. J. & Donachie, W. D. J. Bact. 163, 615–622 (1985).
Taschner, P. E. M., Huls, P. G., Pas, E. & Woldringh, C. L. J. Bact. 170, 1533–1540 (1988).
Yi, Q.-M. & Lutkenhaus, J. Gene 36, 241–247 (1985).
Bi, E. & Lutkenhaus, J. J. Bact. 172, 5602–5609 (1990).
Bourne, H. R., Sanders, D. A. & McCormick, F. Nature 349, 117–127 (1991).
Bourne, H. R., Sanders, D. A. & McCormick, F. Nature 348, 125–132 (1990).
McGrath, J. P., Capon, D. J., Goeddel, D. V. & Levinson, A. D. Nature 310, 644–649 (1984).
Lapetina, E. G. & Reep, B. R. Proc. natn. Acad. Sci. U.S.A. 84, 2261–2265 (1987).
Connolly, T. & Gilmore, R. Cell 57, 599–610 (1989).
Farnsworth, C. L., Marshall, M. S., Gibbs, J. B., Stacey, D. W. & Feig, L. A. Cell 64, 625–633 (1991).
Goud, B., Salminen, A., Walworth, N. C. & Novick, P. J. Cell 53, 753–768 (1988).
Schmitt, H. D., Wagner, P., Pfaff, E. & Gallwitz, D. Cell 47, 401–412 (1986).
Hall, A. & Self, A. J. J. biol. Chem. 261, 10963–10965 (1986).
Hershey, J. W. B. in Escherichia coli & Salmonella typhimurium Cellular & Molecular Biology (eds Neidhardt, F. C. et al. 613–647 (American Society for Microbiology, Washington DC, 1987).
Temeles, G. L., Gibbs, J. B., D'Alonzo, J. S., Sigal, I. S. & Scolnick, E. M. Nature 313, 700–703 (1985).
Poe, M., Scolnick, E. M. & Stein, R. B. J. biol. Chem. 260, 3906–3909 (1985).
Krauhs, E. et al. Proc. natn. Acad. Sci. U.S.A. 78, 4156–4160 (1981).
Oakley, C. E. & Oakley, B. R. Nature 338, 662–664 (1989).
Corton, J. C., Ward, J. E. Jr & Lutkenhaus, J. J. Bact. 169, 1–7 (1987).
Beall, B., Lowe, M. & Lutkenhaus, J. J. Bact. 170, 4855–4864 (1988).
Margolin, W., Corbo, J. C. & Long, S. R. J. Bact. 173, 5822–5830 (1991).
Bender, A. & Pringle, J. R. Proc. natn. Acad. Sci. U.S.A. 86, 9976–9980 (1989).
Chant, J. & Herskowitz, I. Cell 65, 1203–1212 (1991).
Johnson, D. & Pringle, J. R. J. cell Biol. 111, 143–152 (1990).
Chant, J., Corrado, K., Pringle, J. R. & Herskowitz, I. Cell 65, 1213–1224 (1991).
Kim, H. B., Haarer, B. K. & Pringle, J. R. J. cell Biol. 112, 535–544 (1991).
Bi, E. & Lutkenhaus, J. Nature 354, 161–164 (1991).
Janmey, P. A. et al. Nature 347, 95–99 (1990).
McEntee, K., WeinstocK, G. M. & Lehman, I. R. J. biol. Chem. 256, 8835–8844 (1981).
Snyder, J. A. & Mclntosh, J. R. A. Rev. Biochem. 45, 699–720 (1976).
Studier, F. W., Rosenberg, A. H., Dunn, J. J. & Dubendorff, J. W. Meth. Enzym. 185, 60–89 (1990).
Saiki, R. K. et al. Science 239, 487–491 (1988).
Ito, K., Sato, T. & Yura, T. Cell 11, 551–559 (1977).
Rosen, B. P., Weigel, U., Karkaria, C. & Gangola, P. J. biol. Chem. 263, 3067–3070 (1988).
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RayChaudhuri, D., Park, J. Escherichia coli cell-division gene ftsZ encodes a novel GTP-binding protein. Nature 359, 251–254 (1992). https://doi.org/10.1038/359251a0
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DOI: https://doi.org/10.1038/359251a0
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