About: ParM is a research topic. Over the lifetime, 104 publications have been published within this topic receiving 6652 citations. The topic is also known as: ParM-like & IPR042051.
TL;DR: A unique orientation of the monomer with respect to the actin helix has been found and the main interactions are along the two-start helix with a contribution from a loop extending across the filament axis provided by the molecule in the adjacent strand.
Abstract: The F-actin filament has been constructed from the atomic structure of the actin monomer to fit the observed X-ray fibre diagram from oriented gels of F-actin. A unique orientation of the monomer with respect to the actin helix has been found. The main interactions are along the two-start helix with a contribution from a loop extending across the filament axis provided by the molecule in the adjacent strand. There are also contacts along the left-handed genetic helix.
TL;DR: ParM, whose assembly is required for the segregation of large, low–copy number plasmids, displays both dynamic instability and symmetrical, bidirectional polymerization, suggesting that its dynamic instability must have arisen by convergent evolution driven by a set of common constraints on polymer-based segregation of DNA.
Abstract: Dynamic instability-the switching of a two-state polymer between phases of steady elongation and rapid shortening-is essential to the cellular function of eukaryotic microtubules, especially during chromosome segregation. Since the discovery of dynamic instability 20 years ago, no other biological polymer has been found to exhibit this behavior. Using total internal reflection fluorescence microscopy and fluorescence resonance energy transfer, we observe that the prokaryotic actin homolog ParM, whose assembly is required for the segregation of large, low-copy number plasmids, displays both dynamic instability and symmetrical, bidirectional polymerization. The dynamic instability of ParM is regulated by adenosine triphosphate (ATP) hydrolysis, and filaments are stabilized by a cap of ATP-bound monomers. ParM is not related to tubulin, so its dynamic instability must have arisen by convergent evolution driven by a set of common constraints on polymer-based segregation of DNA.
TL;DR: This work reconstituted the three-component segregation system of the R1 plasmid from purified components and found that the ParR/parC complex can construct a simple bipolar spindle by binding the ends of ParM filaments, inhibiting dynamic instability, and acting as a ratchet permitting incorporation of new monomers and riding on the elongating filament ends.
Abstract: Multiple unrelated polymer systems have evolved to partition DNA molecules between daughter cells at division. To better understand polymer-driven DNA segregation, we reconstituted the three-component segregation system of the R1 plasmid from purified components. We found that the ParR/parC complex can construct a simple bipolar spindle by binding the ends of ParM filaments, inhibiting dynamic instability, and acting as a ratchet permitting incorporation of new monomers and riding on the elongating filament ends. Under steady-state conditions, the dynamic instability of unattached ParM filaments provides the energy required to drive DNA segregation.
TL;DR: It is described how prokaryotic actin homologs form mitotic machineries that segregate DNA before cell division, and evidence from three different laboratories indicate that the morphogenetic MreB protein may be involved in segregation of the bacterial chromosome.