Protein-Nanocrystal Conjugates Support a Single Filament Polymerization Model in R1 Plasmid Segregation [electronic resource].
- Berkeley, Calif. : Lawrence Berkeley National Laboratory, 2008.
Oak Ridge, Tenn. : Distributed by the Office of Scientific and Technical Information, U.S. Dept. of Energy.
- Additional Creators:
- Lawrence Berkeley National Laboratory and United States. Department of Energy. Office of Scientific and Technical Information
- Restrictions on Access:
- Free-to-read Unrestricted online access
- To ensure inheritance by daughter cells, many low-copy number bacterial plasmids, including the R1 drug-resistance plasmid, encode their own DNA segregation systems. The par operon of plasmid R1 directs construction of a simple spindle structure that converts free energy of polymerization of an actin-like protein, ParM, into work required to move sister plasmids to opposite poles of rod-shaped cells. The structures of individual components have been solved, but little is known about the ultrastructure of the R1 spindle. To determine the number of ParM filaments in a minimal R1 spindle, we used DNA-gold nanocrystal conjugates as mimics of the R1 plasmid. Wefound that each end of a single polar ParM filament binds to a single ParR/parC-gold complex, consistent with the idea that ParM filaments bind in the hollow core of the ParR/parC ring complex. Our results further suggest that multifilament spindles observed in vivo are associated with clusters of plasmidssegregating as a unit.
- Report Numbers:
- E 1.99:lbnl-1240e
- Other Subject(s):
- Published through SciTech Connect.
Journal of Biological Chemistry 0021-9258 FT
Mullins, R. Dyche; Alivisatos, A. Paul; Claridge, Shelley A.; Choi, Charina L.; Garner, Ethan C.
Materials Sciences Division
- Funding Information:
PN2 EY016546, 5R01GM079556-03
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