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PLoS One. 2015 Mar 18;10(3):e0116414. doi: 10.1371/journal.pone.0116414. eCollection 2015.

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

Author information

1
Laboratoire de Biochimie Théorique, CNRS, UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, 13 rue Pierre et Marie Curie, 75005 Paris, France; MTI, INSERM UMR-M 973, Université Paris Diderot-Paris 7, Bât Lamarck, 35 rue Hélène Brion, 75205 Paris Cedex 13, France.
2
Laboratoire de Biochimie Théorique, CNRS, UPR 9080, Univ Paris Diderot, Sorbonne Paris Cité, 13 rue Pierre et Marie Curie, 75005 Paris, France.
3
DSIMB team, Inserm UMR-S 665 and Univ. Paris Diderot, Sorbonne Paris Cité, INTS, 6 rue Alexandre Cabanel, 75015 Paris, France; Ets Poulain, Pointe-Noire, Republic of Congo.
4
MTI, INSERM UMR-M 973, Université Paris Diderot-Paris 7, Bât Lamarck, 35 rue Hélène Brion, 75205 Paris Cedex 13, France.
5
Technische Universität München, Physik-Department, James-Franck-Str. 1, 85748 Garching, Germany.

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 play a role in homologous recombination. We investigate the variability within each form in terms of helical parameters and steric accessibility. We also address possible helical discontinuities in RecA filaments due to multiple monomer-monomer association modes. By relating local interface organization to global filament morphology, the strategies developed here to study RecA self-assembly are particularly well suited to other DNA-binding proteins and to filamentous protein assemblies in general.

PMID:
25785454
PMCID:
PMC4364692
DOI:
10.1371/journal.pone.0116414
[Indexed for MEDLINE]
Free PMC Article

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