4.6 Article

Protein-nanocrystal conjugates support a single filament polymerization model in R1 plasmid segregation

Journal

JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 283, Issue 42, Pages 28081-28086

Publisher

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M803833200

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Funding

  1. National Institutes of Health [PN2 EY016546, 5R01GM079556-03]
  2. University of California San Francisco/University of California Berkeley Nanomedicine Development Center
  3. University of California San Francisco
  4. Sandler Family Supporting Foundation
  5. 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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