- Physical Review Journals
All JournalsPhysics Magazine
Access Provided by Xinjiang University

Physical Review E

Export citation

Export citation

Choose format for download:

Download Citation
  • Access by Xinjiang University

Force generation in bacteria without nucleotide-dependent bending of cytoskeletal filaments

Biplab Ghosh* and Anirban Sain†

  • Department of Physics, Indian Institute of Technology-Bombay, Powai, Mumbai 400 085, India

  • *Also at Theoretical Physics Division, Bhabha Atomic Research Centre, Trombay, Mumbai 400 085, India.
  • †asain@phy.iitb.ac.in
PDF

Phys. Rev. E 83, 051924 – Published 27 May, 2011

DOI: https://doi.org/10.1103/PhysRevE.83.051924

Abstract

Binary cell division in bacteria occurs via the formation and subsequent contraction of a polymeric ring, the so-called Z ring, at the middle of the cell. This ring is made of filamenting temperature-sensitive Z (FtsZ) proteins and it shrinks in radius to generate a contractile radial force on the cell membrane. Although a few models have been proposed, the ring contraction mechanism still remains a mystery. The models rely on various physical properties of the FtsZ filaments, some of which have been verified through in vitro experiments and some of which remain unclear. A feature common to all these models is the hydrolysis-driven transition of FtsZ filaments from straight to curved conformations. While the intrinsic curvature of FtsZ filaments has been experimentally established beyond doubt, evidence has been mounting against the existence of any transition between the straight FtsZ-GTP and the curved FtsZ-GDP conformations. Preliminary results from our earlier work [B. Ghosh and A. Sain, Phys. Rev. Lett. 101, 178101 (2008)] indicated that hydrolysis-induced bending is not necessary for Z-ring contraction. Since then many new experimental observations have been reported on this subject and in view of these here we argue that our model appears even more plausible than before. In addition, we have explored more realistic features, such as how the length distribution of FtsZ filaments in the cytoplasm may influence the contraction dynamics, and we have also demonstrated that the Z ring retains approximately the same number of monomers, although not the same monomers, during the course of contraction as reported by fluorescence experiments.

    View figure in article

      Article Text

      References (27)

      1. J. Lutkenhaus, Annu. Rev. Biochem. 76, 539 (2007).
      2. B. Ghosh and A. Sain, Phys. Rev. Lett. 101, 178101 (2008).
      3. G. Lan, C. W. Wolgemuth, and S. X. Sun, Proc. Natl. Acad. Sci. U.S.A. 104, 16110 (2007).
      4. J. F. Allard and E. N. Cytrynbaum, Proc. Natl. Acad. Sci. U.S.A. 106, 145 (2009).
      5. G. Lan, B. R. Daniels, T. M. Dobrowsky, D. Wirtz, and S. X. Sun, Proc. Natl. Acad. Sci. U.S.A. 106, 121 (2009).
      6. Z. Li, M. J. Trimble, Y. V. Brun, and G. J. Jensen, EMBO J. 26, 4694 (2007).
      7. H. P. Erickson, Proc. Natl. Acad. Sci. U.S.A. 106, 9238 (2009).
      8. M. Osawa, D. E. Anderson, and H. P. Erickson, Science 320, 792 (2008).
      9. H. P. Erickson, D. W. Taylor, K. A. Taylor, and D. Bramhill, Proc. Natl. Acad. Sci. U.S.A. 93, 519 (1996).
      10. J. Mingorance, M. Tadros, M. Vicente, J. M. González, G. Rivas, and M. Vélez, J. Biol. Chem. 280, 20909 (2005).
      11. R. Srinivasan, M. Mishra, L. Wu, Z. Yin, and M. K. Balasubramanian, Genes Dev. 22, 1741 (2008).
      12. M. Osawa, D. E. Anderson, and H. P. Erickson, EMBO J. 28, 3476 (2009).
      13. M. A. Oliva, D. Trambaiolo, and J. Lowe, J. Mol. Biol. 373, 1229 (2007).
      14. I. Hörger, E. Velasco, J. Mingorance, G. Rivas, P. Tarazona, and M. Vélez, Phys. Rev. E 77, 011902 (2008).
      15. D. Popp, M. Iwasa, A. Narita, H. P. Erickson, and Y. Maeda, Biopolymers 91, 340 (2009).
      16. Q. Sun and W. Margolin, J. Bacteriol. 180, 2050 (1998).
      17. X. Wang, C. Possoz, and D. J. Sherratt, Genes Dev. 19, 2367 (2005).
      18. G. Fu, T. Huang, J. Buss, C. Coltharp, Z. Hensel, and J. Xiao, PLoS One 5, e12680 (2010).
      19. J. M. González, M. Jiménez, M. Vélez, J. Mingorance, J. M. Andreu, M. Vicente, and G. Rivas, J. Biol. Chem. 278, 37664 (2003).
      20. J. Stricker, P. Maddox, E. D. Salmon, and H. P. Erickson, Proc. Natl. Acad. Sci. U.S.A. 99, 3171 (2002).
      21. G. Lan, A. Dajkovic, D. Wirtz, and S. X. Sun, Biophys J. 95, 4045 (2008).
      22. J. M. González, M. Vélez, M. Jiménez, C. Alfonso, P. Schuck, J. Mingorance, M. Vicente, A. P. Minton, and G. Rivas, Proc. Natl. Acad. Sci. U.S.A. 102, 1895 (2005).
      23. S. Huecas and J. M. Andreu, J. Biol. Chem. 278, 46146 (2003).
      24. A. L. Barabasi and H. E. Stanley, Fractal Concepts in Surface Growth (Cambridge University, Cambridge, U.K., 1995).
      25. P. C. Peters, M. D. Migocki, C. Thoni, and E. J. Harry, Mol. Microbiol. 64, 487 (2007).
      26. L. G. Monahan, A. Robinson, and E. J. Harry, Mol. Microbiol. 74, 1004 (2009).
      27. G. Reshes, S. Vanounou, I. Fishov, and M. Feingold, Biophys J. 94, 251 (2008).

      Outline

      Information

      Phys. Rev. E 83, 051924– Published 27 May, 2011
      • Received 7 June 2010

      ©2011 American Physical Society

      Sign In to Your Journals Account

      Filter

      Filter

      Article Lookup

      Enter a citation