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.

Science 2 March 2007:
Vol. 315. no. 5816, pp. 1270 - 1274
DOI: 10.1126/science.1138527
Prev | Table of Contents | Next

Reports

Reconstitution of DNA Segregation Driven by Assembly of a Prokaryotic Actin Homolog

Ethan C. Garner,1,2,3 Christopher S. Campbell,1,2,3 Douglas B. Weibel,3,4 R. Dyche Mullins1,2,3*

Multiple unrelated polymer systems have evolved to partition DNA molecules between daughter cells at division. To better understand polymer-driven DNA segregation, we reconstituted the three-component segregation system of the R1 plasmid from purified components. We found that the ParR/parC complex can construct a simple bipolar spindle by binding the ends of ParM filaments, inhibiting dynamic instability, and acting as a ratchet permitting incorporation of new monomers and riding on the elongating filament ends. Under steady-state conditions, the dynamic instability of unattached ParM filaments provides the energy required to drive DNA segregation.

1 Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94158, USA.
2 UCSF/UCB Nanomedicine Development Center, San Francisco, CA 94158, USA.
3 Physiology Course, Marine Biological Laboratory, Woods Hole, MA02543, USA.
4 Department of Biochemistry, University of Wisconsin, Madison, WI 53706, USA.

* To whom correspondence should be addressed. E-mail: dyche{at}mullinslab.ucsf.edu

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
A Biosensor for Fluorescent Determination of ADP with High Time Resolution.
S. Kunzelmann and M. R. Webb (2009)
J. Biol. Chem. 284, 33130-33138
   Abstract »    Full Text »    PDF »
Dual Role of DNA in Regulating ATP Hydrolysis by the SopA Partition Protein.
Y. Ah-Seng, F. Lopez, F. Pasta, D. Lane, and J.-Y. Bouet (2009)
J. Biol. Chem. 284, 30067-30075
   Abstract »    Full Text »    PDF »
The Structure and Assembly Dynamics of Plasmid Actin AlfA Imply a Novel Mechanism of DNA Segregation.
J. K. Polka, J. M. Kollman, D. A. Agard, and R. D. Mullins (2009)
J. Bacteriol. 191, 6219-6230
   Abstract »    Full Text »    PDF »
Recruitment of the ParG Segregation Protein to Different Affinity DNA Sites.
M. Zampini, A. Derome, S. E. S. Bailey, D. Barilla, and F. Hayes (2009)
J. Bacteriol. 191, 3832-3841
   Abstract »    Full Text »    PDF »
The Tubulin-Like RepX Protein Encoded by the pXO1 Plasmid Forms Polymers In Vivo in Bacillus anthracis.
P. Akhtar, S. P. Anand, S. C. Watkins, and S. A. Khan (2009)
J. Bacteriol. 191, 2493-2500
   Abstract »    Full Text »    PDF »
Electron Cryomicroscopy of E. coli Reveals Filament Bundles Involved in Plasmid DNA Segregation.
J. Salje, B. Zuber, and J. Lowe (2009)
Science 323, 509-512
   Abstract »    Full Text »    PDF »
Protein-Nanocrystal Conjugates Support a Single Filament Polymerization Model in R1 Plasmid Segregation.
C. L. Choi, S. A. Claridge, E. C. Garner, A. P. Alivisatos, and R. D. Mullins (2008)
J. Biol. Chem. 283, 28081-28086
   Abstract »    Full Text »    PDF »
Caulobacter requires a dedicated mechanism to initiate chromosome segregation.
E. Toro, S.-H. Hong, H. H. McAdams, and L. Shapiro (2008)
PNAS 105, 15435-15440
   Abstract »    Full Text »    PDF »
Streptococcus pyogenes pSM19035 requires dynamic assembly of ATP-bound ParA and ParB on parS DNA during plasmid segregation.
F. Pratto, A. Cicek, W. A. Weihofen, R. Lurz, W. Saenger, and J. C. Alonso (2008)
Nucleic Acids Res. 36, 3676-3689
   Abstract »    Full Text »    PDF »
In Vitro Assembly Studies of FtsZ/Tubulin-like Proteins (TubZ) from Bacillus Plasmids: EVIDENCE FOR A CAPPING MECHANISM.
Y. Chen and H. P. Erickson (2008)
J. Biol. Chem. 283, 8102-8109
   Abstract »    Full Text »    PDF »
Bacterial Growth and Cell Division: a Mycobacterial Perspective.
E. C. Hett and E. J. Rubin (2008)
Microbiol. Mol. Biol. Rev. 72, 126-156
   Abstract »    Full Text »    PDF »
Centromere anatomy in the multidrug-resistant pathogen Enterococcus faecium.
A. Derome, C. Hoischen, M. Bussiek, R. Grady, M. Adamczyk, B. Keedzierska, S. Diekmann, D. Barilla, and F. Hayes (2008)
PNAS 105, 2151-2156
   Abstract »    Full Text »    PDF »
Escherichia coli low-copy-number plasmid R1 centromere parC forms a U-shaped complex with its binding protein ParR.
C. Hoischen, M. Bussiek, J. Langowski, and S. Diekmann (2008)
Nucleic Acids Res. 36, 607-615
   Abstract »    Full Text »    PDF »
Plasmid segregation: spatial awareness at the molecular level.
J. Moller-Jensen and K. Gerdes (2007)
J. Cell Biol. 179, 813-815
   Abstract »    Full Text »    PDF »
In vivo visualization of type II plasmid segregation: bacterial actin filaments pushing plasmids.
C. S. Campbell and R. D. Mullins (2007)
J. Cell Biol. 179, 1059-1066
   Abstract »    Full Text »    PDF »
Distribution of Centromere-Like parS Sites in Bacteria: Insights from Comparative Genomics.
J. Livny, Y. Yamaichi, and M. K. Waldor (2007)
J. Bacteriol. 189, 8693-8703
   Abstract »    Full Text »    PDF »
Changes in Nucleoid Morphology and Origin Localization upon Inhibition or Alteration of the Actin Homolog, MreB, of Vibrio cholerae.
P. Srivastava, G. Demarre, T. S. Karpova, J. McNally, and D. K. Chattoraj (2007)
J. Bacteriol. 189, 7450-7463
   Abstract »    Full Text »    PDF »
Centromere Pairing by a Plasmid-encoded Type I ParB Protein.
S. Ringgaard, J. Lowe, and K. Gerdes (2007)
J. Biol. Chem. 282, 28216-28225
   Abstract »    Full Text »    PDF »
Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis.
R. A. Larsen, C. Cusumano, A. Fujioka, G. Lim-Fong, P. Patterson, and J. Pogliano (2007)
Genes & Dev. 21, 1340-1352
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

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