This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lu, C.
Right arrow Articles by Erickson, H. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lu, C.
Right arrow Articles by Erickson, H. P.

 Previous Article  |  Next Article 

Journal of Bacteriology, January 2000, p. 164-170, Vol. 182, No. 1
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Straight and Curved Conformations of FtsZ Are Regulated by GTP Hydrolysis

Chunlin Lu, Mary Reedy, and Harold P. Erickson*

Department of Cell Biology, Duke University Medical Center, Durham, North Carolina 27710

Received 31 March 1999/Accepted 4 October 1999

FtsZ assembles in vitro into protofilaments that can adopt two conformations---the straight conformation, which can assemble further into two-dimensional protofilament sheets, and the curved conformation, which forms minirings about 23 nm in diameter. Here, we describe the structure of FtsZ tubes, which are a variation of the curved conformation. In the tube the curved protofilament forms a shallow helix with a diameter of 23 nm and a pitch of 18 or 24°. We suggest that this shallow helix is the relaxed structure of the curved protofilament in solution. We provide evidence that GTP favors the straight conformation while GDP favors the curved conformation. In particular, exclusively straight protofilaments and protofilament sheets are assembled in GMPCPP, a nonhydrolyzable GTP analog, or in GTP following chelation of Mg, which blocks GTP hydrolysis. Assembly in GDP produces exclusively tubes. The transition from straight protofilaments to the curved conformation may provide a mechanism whereby the energy of GTP hydrolysis is used to generate force for the constriction of the FtsZ ring in cell division.

* Corresponding author. Mailing address: Department of Cell Biology, 3011, Duke University Medical Center, Durham, NC 27710. Phone: (919) 684-6385. Fax: (919) 684-3687. E-mail: H.Erickson{at}cellbio.duke.edu.

Journal of Bacteriology, January 2000, p. 164-170, Vol. 182, No. 1
0021-9193/0/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Erickson, H. P. (2009). Modeling the physics of FtsZ assembly and force generation. Proc. Natl. Acad. Sci. USA 106: 9238-9243 [Abstract] [Full Text]  
  • Allard, J. F., Cytrynbaum, E. N. (2009). Force generation by a dynamic Z-ring in Escherichia coli cell division. Proc. Natl. Acad. Sci. USA 106: 145-150 [Abstract] [Full Text]  
  • Srinivasan, R., Mishra, M., Wu, L., Yin, Z., Balasubramanian, M. K. (2008). The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast. Genes Dev. 22: 1741-1746 [Abstract] [Full Text]  
  • Osawa, M., Anderson, D. E., Erickson, H. P. (2008). Reconstitution of Contractile FtsZ Rings in Liposomes. Science 320: 792-794 [Abstract] [Full Text]  
  • Dajkovic, A., Mukherjee, A., Lutkenhaus, J. (2008). Investigation of Regulation of FtsZ Assembly by SulA and Development of a Model for FtsZ Polymerization. J. Bacteriol. 190: 2513-2526 [Abstract] [Full Text]  
  • Cabeen, M. T., Jacobs-Wagner, C. (2007). Skin and bones: the bacterial cytoskeleton, cell wall, and cell morphogenesis. JCB 179: 381-387 [Abstract] [Full Text]  
  • Carballido-Lopez, R. (2006). The Bacterial Actin-Like Cytoskeleton. Microbiol. Mol. Biol. Rev. 70: 888-909 [Abstract] [Full Text]  
  • Osawa, M., Erickson, H. P. (2006). FtsZ from Divergent Foreign Bacteria Can Function for Cell Division in Escherichia coli.. J. Bacteriol. 188: 7132-7140 [Abstract] [Full Text]  
  • Lohse, S., Hause, B., Hause, G., Fester, T. (2006). FtsZ Characterization and Immunolocalization in the Two Phases of Plastid Reorganization in Arbuscular Mycorrhizal Roots of Medicago truncatula. Plant Cell Physiol 47: 1124-1134 [Abstract] [Full Text]  
  • Esue, O., Wirtz, D., Tseng, Y. (2006). GTPase Activity, Structure, and Mechanical Properties of Filaments Assembled from Bacterial Cytoskeleton Protein MreB. J. Bacteriol. 188: 968-976 [Abstract] [Full Text]  
  • Sontag, C. A., Staley, J. T., Erickson, H. P. (2005). In vitro assembly and GTP hydrolysis by bacterial tubulins BtubA and BtubB. JCB 169: 233-238 [Abstract] [Full Text]  
  • Marrington, R., Small, E., Rodger, A., Dafforn, T. R., Addinall, S. G. (2004). FtsZ Fiber Bundling Is Triggered by a Conformational Change in Bound GTP. J. Biol. Chem. 279: 48821-48829 [Abstract] [Full Text]  
  • Santra, M. K., Beuria, T. K., Banerjee, A., Panda, D. (2004). Ruthenium Red-induced Bundling of Bacterial Cell Division Protein, FtsZ. J. Biol. Chem. 279: 25959-25965 [Abstract] [Full Text]  
  • Fiebig, A., Theriot, J. A. (2004). Bacteria make tracks to the pole. Proc. Natl. Acad. Sci. USA 101: 8510-8511 [Full Text]  
  • Ferguson, P. L., Shaw, G. S. (2004). Human S100B Protein Interacts with the Escherichia coli Division Protein FtsZ in a Calcium-sensitive Manner. J. Biol. Chem. 279: 18806-18813 [Abstract] [Full Text]  
  • Ohashi, T., Erickson, H. P. (2004). The Disulfide Bonding Pattern in Ficolin Multimers. J. Biol. Chem. 279: 6534-6539 [Abstract] [Full Text]  
  • Huecas, S., Andreu, J. M. (2003). Energetics of the Cooperative Assembly of Cell Division Protein FtsZ and the Nucleotide Hydrolysis Switch. J. Biol. Chem. 278: 46146-46154 [Abstract] [Full Text]  
  • Stricker, J., Erickson, H. P. (2003). In Vivo Characterization of Escherichia coli ftsZ Mutants: Effects on Z-Ring Structure and Function. J. Bacteriol. 185: 4796-4805 [Abstract] [Full Text]  
  • Small, E., Addinall, S. G. (2003). Dynamic FtsZ polymerization is sensitive to the GTP to GDP ratio and can be maintained at steady state using a GTP-regeneration system. Microbiology 149: 2235-2242 [Abstract] [Full Text]  
  • Errington, J., Daniel, R. A., Scheffers, D.-J. (2003). Cytokinesis in Bacteria. Microbiol. Mol. Biol. Rev. 67: 52-65 [Abstract] [Full Text]  
  • Beuria, T. K., Krishnakumar, S. S., Sahar, S., Singh, N., Gupta, K., Meshram, M., Panda, D. (2003). Glutamate-induced Assembly of Bacterial Cell Division Protein FtsZ. J. Biol. Chem. 278: 3735-3741 [Abstract] [Full Text]  
  • Andreu, J. M., Oliva, M. A., Monasterio, O. (2002). Reversible Unfolding of FtsZ Cell Division Proteins from Archaea and Bacteria. COMPARISON WITH EUKARYOTIC TUBULIN FOLDING AND ASSEMBLY. J. Biol. Chem. 277: 43262-43270 [Abstract] [Full Text]  
  • Gueiros-Filho, F. J., Losick, R. (2002). A widely conserved bacterial cell division protein that promotes assembly of the tubulin-like protein FtsZ. Genes Dev. 16: 2544-2556 [Abstract] [Full Text]  
  • Stricker, J., Maddox, P., Salmon, E. D., Erickson, H. P. (2002). Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. USA 10.1073/pnas.052595099v1 [Abstract] [Full Text]  
  • McAndrew, R. S., Froehlich, J. E., Vitha, S., Stokes, K. D., Osteryoung, K. W. (2001). Colocalization of Plastid Division Proteins in the Chloroplast Stromal Compartment Establishes a New Functional Relationship between FtsZ1 and FtsZ2 in Higher Plants. Plant Physiol. 127: 1656-1666 [Abstract] [Full Text]  
  • Miyagishima, S.-y., Takahara, M., Mori, T., Kuroiwa, H., Higashiyama, T., Kuroiwa, T. (2001). Plastid Division Is Driven by a Complex Mechanism That Involves Differential Transition of the Bacterial and Eukaryotic Division Rings. Plant Cell 13: 2257-2268 [Abstract] [Full Text]  
  • Miyagishima, S.-y., Takahara, M., Kuroiwa, T. (2001). Novel Filaments 5 nm in Diameter Constitute the Cytosolic Ring of the Plastid Division Apparatus. Plant Cell 13: 707-721 [Abstract] [Full Text]  
  • McFadden, G. I. (2000). Skeletons in the Closet: How Do Chloroplasts Stay in Shape?. JCB 151: f19-f22 [Full Text]  
  • Hale, C. A., Rhee, A. C., de Boer, P. A. J. (2000). ZipA-Induced Bundling of FtsZ Polymers Mediated by an Interaction between C-Terminal Domains. J. Bacteriol. 182: 5153-5166 [Abstract] [Full Text]  
  • Osteryoung, K. W. (2000). Organelle Fission. Crossing the Evolutionary Divide. Plant Physiol. 123: 1213-1216 [Full Text]  
  • White, E. L., Ross, L. J., Reynolds, R. C., Seitz, L. E., Moore, G. D., Borhani, D. W. (2000). Slow Polymerization of Mycobacterium tuberculosis FtsZ. J. Bacteriol. 182: 4028-4034 [Abstract] [Full Text]  
  • Erickson, H. P. (2000). Dynamin and Ftsz: Missing Links in Mitochondrial and Bacterial Division. JCB 148: 1103-1106 [Full Text]  
  • Romberg, L., Simon, M., Erickson, H. P. (2001). Polymerization of FtsZ, a Bacterial Homolog of Tubulin. IS ASSEMBLY COOPERATIVE?. J. Biol. Chem. 276: 11743-11753 [Abstract] [Full Text]  
  • Diaz, J. F., Kralicek, A., Mingorance, J., Palacios, J. M., Vicente, M., Andreu, J. M. (2001). Activation of Cell Division Protein FtsZ. CONTROL OF SWITCH LOOP T3 CONFORMATION BY THE NUCLEOTIDE gamma -PHOSPHATE. J. Biol. Chem. 276: 17307-17315 [Abstract] [Full Text]  
  • Stricker, J., Maddox, P., Salmon, E. D., Erickson, H. P. (2002). Rapid assembly dynamics of the Escherichia coli FtsZ-ring demonstrated by fluorescence recovery after photobleaching. Proc. Natl. Acad. Sci. USA 99: 3171-3175 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»