Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Originally published In Press as doi:10.1074/jbc.M703788200 on July 20, 2007

J. Biol. Chem., Vol. 282, Issue 38, 27736-27743, September 21, 2007
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow All Versions of this Article:
282/38/27736    most recent
M703788200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
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 arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Chen, Y.
Right arrow Articles by Erickson, H. P.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Chen, Y.
Right arrow Articles by Erickson, H. P.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Assembly Dynamics of Mycobacterium tuberculosis FtsZ*

Yaodong Chen{ddagger}, David E. Anderson{ddagger}, Malini Rajagopalan§, and Harold P. Erickson{ddagger}1

From the {ddagger}Department of Cell Biology, Duke University, Medical Center, Durham, North Carolina 27710 and §Biomedical Research, University of Texas Health Center, Tyler, Texas 75708-3154

We have investigated the assembly of FtsZ from Mycobacterium tuberculosis (MtbFtsZ). Electron microscopy confirmed the previous observation that MtbFtsZ assembled into long, two-stranded filaments at pH 6.5. However, we found that assembly at pH 7.2 or 7.7 produced predominantly short, one-stranded protofilaments, similar to those of Escherichia coli FtsZ (EcFtsZ). Near pH 7, which is close to the pH of M. tuberculosis cytoplasm, MtbFtsZ formed a mixture of single- and two-stranded filaments. We developed a fluorescence resonance energy transfer assay to measure the kinetics of initial assembly and the dynamic properties at steady state. Assembly of MtbFtsZ reached a plateau after 60–100 s, about 10 times slower than EcFtsZ. The initial assembly kinetics were similar at pH 6.5 and 7.7, despite the striking difference in the polymer structures. Both were fit with a cooperative assembly mechanism involving a weak dimer nucleus, similar to EcFtsZ but with slower kinetics. Subunit turnover and GTPase at steady state were also about 10 times slower for MtbFtsZ than for EcFtsZ. Specifically, the half-time for subunit turnover in vitro at pH 7.7 was 42 s for MtbFtsZ compared with 5.5 s for EcFtsZ. Photobleaching studies in vivo showed a range of turnover half-times with an average of 25 s for MtbFtsZ as compared with 9 s for EcFtsZ.


Received for publication, May 8, 2007 , and in revised form, June 24, 2007.

* This work was supported by National Institutes of Health Grants GM66014 (to H. P. E.) and AI48417 and AI64502 (to M. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

1 To whom correspondence should be addressed: Dept. of Cell Biology, Duke University Medical Center, Box 3709, Durham, NC 27710. Tel.: 919-684-6385; Fax: 919-684-8090; E-mail: h.erickson{at}cellbio.duke.edu.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
Biophys. JHome page
G. Lan, A. Dajkovic, D. Wirtz, and S. X. Sun
Polymerization and Bundling Kinetics of FtsZ Filaments
Biophys. J., October 15, 2008; 95(8): 4045 - 4056.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
E. R. Miraldi, P. J. Thomas, and L. Romberg
Allosteric Models for Cooperative Polymerization of Linear Polymers
Biophys. J., September 1, 2008; 95(5): 2470 - 2486.
[Abstract] [Full Text] [PDF]


Home page
Genes Dev.Home page
R. Srinivasan, M. Mishra, L. Wu, Z. Yin, and M. K. Balasubramanian
The bacterial cell division protein FtsZ assembles into cytoplasmic rings in fission yeast
Genes & Dev., July 1, 2008; 22(13): 1741 - 1746.
[Abstract] [Full Text] [PDF]


Home page
Biophys. JHome page
S. Huecas, O. Llorca, J. Boskovic, J. Martin-Benito, J. M. Valpuesta, and J. M. Andreu
Energetics and Geometry of FtsZ Polymers: Nucleated Self-Assembly of Single Protofilaments
Biophys. J., March 1, 2008; 94(5): 1796 - 1806.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
S. Huecas, C. Schaffner-Barbero, W. Garcia, H. Yebenes, J. M. Palacios, J. F. Diaz, M. Menendez, and J. M. Andreu
The Interactions of Cell Division Protein FtsZ with Guanine Nucleotides
J. Biol. Chem., December 28, 2007; 282(52): 37515 - 37528.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2007 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement