Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Published Online April 17, 2008
Science DOI: 10.1126/science.1154520

Reports

Submitted on December 21, 2007
Accepted on February 25, 2008

Reconstitution of Contractile FtsZ Rings in Liposomes

Masaki Osawa 1, David E. Anderson 1, Harold P. Erickson 1*

1 Department of Cell Biology, Duke University Medical Center, Durham, NC 27710-3709, USA.

* To whom correspondence should be addressed.
Harold P. Erickson , E-mail: h.erickson{at}cellbio.duke.edu

FtsZ is a tubulin homolog and the major cytoskeletal protein in bacterial cell division. It assembles into the Z ring, which contains FtsZ and a dozen other division proteins, and constricts to divide the cell. We have constructed a membrane-targeted FtsZ (FtsZ-mts) by splicing an amphipathic helix to its C terminus. When mixed with lipid vesicles, FtsZ-mts was incorporated into the interior of some tubular vesicles. There it formed multiple Z rings that could move laterally in both directions along the length of the liposome, and coalesce into brighter Z rings. Brighter Z rings produced visible constrictions in the liposome, suggesting that FtsZ itself can assemble the Z ring and generate a force. No other proteins were needed for assembly and force generation.


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
Actin, a Central Player in Cell Shape and Movement.
T. D. Pollard and J. A. Cooper (2009)
Science 326, 1208-1212
   Abstract »    Full Text »    PDF »
Targeted Gene Knockouts Reveal Overlapping Functions of the Five Physcomitrella patens FtsZ Isoforms in Chloroplast Division, Chloroplast Shaping, Cell Patterning, Plant Development, and Gravity Sensing.
A. Martin, D. Lang, S. T. Hanke, S. J.X. Mueller, E. Sarnighausen, M. Vervliet-Scheebaum, and R. Reski (2009)
Mol Plant 2, 1359-1372
   Abstract »    Full Text »    PDF »
Arabidopsis FtsZ2-1 and FtsZ2-2 Are Functionally Redundant, But FtsZ-Based Plastid Division Is Not Essential for Chloroplast Partitioning or Plant Growth and Development.
A. J. Schmitz, J. M. Glynn, B. J.S.C. Olson, K. D. Stokes, and K. W. Osteryoung (2009)
Mol Plant 2, 1211-1222
   Abstract »    Full Text »    PDF »
Structural Plasticity in Actin and Tubulin Polymer Dynamics.
H. Y. Kueh and T. J. Mitchison (2009)
Science 325, 960-963
   Abstract »    Full Text »    PDF »
ATP-Binding Site Lesions in FtsE Impair Cell Division.
S. J. R. Arends, R. J. Kustusch, and D. S. Weiss (2009)
J. Bacteriol. 191, 3772-3784
   Abstract »    Full Text »    PDF »
Modeling the physics of FtsZ assembly and force generation.
H. P. Erickson (2009)
PNAS 106, 9238-9243
   Abstract »    Full Text »    PDF »
Force generation by a dynamic Z-ring in Escherichia coli cell division.
J. F. Allard and E. N. Cytrynbaum (2009)
PNAS 106, 145-150
   Abstract »    Full Text »    PDF »
Condensation of FtsZ filaments can drive bacterial cell division.
G. Lan, B. R. Daniels, T. M. Dobrowsky, D. Wirtz, and S. X. Sun (2009)
PNAS 106, 121-126
   Abstract »    Full Text »    PDF »
Bacillus subtilis MinC destabilizes FtsZ-rings at new cell poles and contributes to the timing of cell division.
J. A. Gregory, E. C. Becker, and K. Pogliano (2008)
Genes & Dev. 22, 3475-3488
   Abstract »    Full Text »    PDF »
Proteome-Based Comparative Analyses of Growth Stages Reveal New Cell Cycle-Dependent Functions in the Predatory Bacterium Bdellovibrio bacteriovorus.
M. Dori-Bachash, B. Dassa, S. Pietrokovski, and E. Jurkevitch (2008)
Appl. Envir. Microbiol. 74, 7152-7162
   Abstract »    Full Text »    PDF »
SepF Increases the Assembly and Bundling of FtsZ Polymers and Stabilizes FtsZ Protofilaments by Binding along Its Length.
J. K. Singh, R. D. Makde, V. Kumar, and D. Panda (2008)
J. Biol. Chem. 283, 31116-31124
   Abstract »    Full Text »    PDF »
Four proteins, two new cells.
R. Robinson (2008)
J. Cell Biol. 181, 714
   Full Text »    PDF »
Arabidopsis ARC6 Coordinates the Division Machineries of the Inner and Outer Chloroplast Membranes through Interaction with PDV2 in the Intermembrane Space.
J. M. Glynn, J. E. Froehlich, and K. W. Osteryoung (2008)
PLANT CELL 20, 2460-2470
   Abstract »    Full Text »    PDF »
The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast.
R. Srinivasan, M. Mishra, L. Wu, Z. Yin, and M. K. Balasubramanian (2008)
Genes & Dev. 22, 1741-1746
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)