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

PloS One
Benjamin BoyerChantal Prévost

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 prote...Continue Reading

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Citations

Feb 13, 2016·Scientific Reports·Linh TranTâp Ha-Duong
Oct 16, 2015·Critical Reviews in Biochemistry and Molecular Biology·Mara PrentissClaudia Danilowicz
Aug 3, 2019·Nucleic Acids Research·Benjamin BoyerChantal Prévost
Jul 15, 2016·Physical Review. E·Sergio Cruz LeónMaria Fyta

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Methods Mentioned

BETA
electron
X-ray
electron microscopy
AFM

Software Mentioned

PyATTRACT
ATTRACT
PITA
RecA
PISA
NACCESS
PTools
Heligeom
PTools Python / C +
3CMW

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