F‐actin‐like filaments formed by plasmid segregation protein ParM

@article{vandenEnt2002FactinlikeFF,
  title={F‐actin‐like filaments formed by plasmid segregation protein ParM},
  author={Fusinita M. I. van den Ent and Jakob M{\o}ller-Jensen and Linda A Amos and Kenn Gerdes and Jan L{\"o}we},
  journal={The EMBO Journal},
  year={2002},
  volume={21}
}
It was the general belief that DNA partitioning in prokaryotes is independent of a cytoskeletal structure, which in eukaryotic cells is indispensable for DNA segregation. Recently, however, immunofluorescence microscopy revealed highly dynamic, filamentous structures along the longitudinal axis of Escherichia coli formed by ParM, a plasmid‐encoded protein required for accurate segregation of low‐copy‐number plasmid R1. We show here that ParM polymerizes into double helical protofilaments with a… 
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TLDR
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TLDR
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TLDR
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TLDR
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Microtubule-like Properties of the Bacterial Actin Homolog ParM-R1*
TLDR
It is shown that actin homolog, ParM-R1 that drives segregation of the R1 multidrug resistance plasmid from Escherichia coli, can also self-organize in vitro into asters, which resemble astral microtubules, which imply that the selection pressure to reliably segregate DNA during cell division has led to common mechanisms within diverse segregation machineries.
Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF
TLDR
It is shown that the ParF partition protein specified by the TP228 plasmid is a ParA ATPase that assembles into extensive filaments in vitro that points to an evolutionary parallel between DNA segregation and cytokinesis in prokaryotic cells, and reveals a potential molecular mechanism forplasmid and chromosome segregation mediated by the ubiquitous ParA‐type proteins.
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