Unknown

Dataset Information

0

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


ABSTRACT: 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.

SUBMITTER: Choi CL 

PROVIDER: S-EPMC2568930 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC3926056 | biostudies-literature
| S-EPMC6400962 | biostudies-literature
| S-EPMC2843175 | biostudies-literature
| S-EPMC5645730 | biostudies-literature
| S-EPMC2978586 | biostudies-literature
| S-EPMC4949242 | biostudies-literature
| S-EPMC5179141 | biostudies-literature
| S-EPMC6333216 | biostudies-literature
| S-EPMC4415385 | biostudies-literature
| S-EPMC1070370 | biostudies-literature