An integrative approach to the study of filamentous oligomeric assemblies, with application to RecA.

ABSTRACT: Oligomeric macromolecules in the cell self-organize into a wide variety of geometrical motifs such as helices, rings or linear filaments. The recombinase proteins involved in homologous recombination present many such assembly motifs. Here, we examine in particular the polymorphic characteristics of RecA, the most studied member of the recombinase family, using an integrative approach that relates local modes of monomer/monomer association to the global architecture of their screw-type organization. In our approach, local modes of association are sampled via docking or Monte Carlo simulations. This enables shedding new light on fiber morphologies that may be adopted by the RecA protein. Two distinct RecA helical morphologies, the so-called "extended" and "compressed" forms, are known to pl

SUBMITTER: Boyer B 

PROVIDER: S-EPMC4364692 | biostudies-literature | 2015

REPOSITORIES: biostudies-literature