Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 42, Pages 28081-28086Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M803833200
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Funding
- National Institutes of Health [PN2 EY016546, 5R01GM079556-03]
- University of California San Francisco/University of California Berkeley Nanomedicine Development Center
- University of California San Francisco
- Sandler Family Supporting Foundation
- Office of Science, Office of Basic Energy Sciences, of the United States Department of Energy [DE-AC02-05CH11231]
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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. We found 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 plasmids segregating as a unit.
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