Human Rad51 mediated DNA unwinding is facilitated by conditions that favour Rad51-dsDNA aggregation.

BMC Biochemistry
Kamakshi BalakrishnanBasuthkar J Rao

Abstract

Human Rad51 (RAD51), analogous to its bacterial homolog, RecA, binds and unwinds double stranded DNA (dsDNA) in the presence of certain nucleotide cofactors. ATP hydrolysis is not required for this process, because even ATP non hydrolysable analogs like AMP-PNP and ATPgammaS, support DNA unwinding. Even ADP, the product of ATP hydrolysis, feebly supports DNA unwinding. We find that human Rad52 (RAD52) stimulates RAD51 mediated DNA unwinding in the presence of all Adenine nucleotide cofactors, (except in AMP and no nucleotide conditions that intrinsically fail to support unwinding reaction) while enhancing aggregation of RAD51-dsDNA complexes in parallel. Interestingly, salt at low concentration can substitute the role of RAD52, in facilitating aggregation of RAD51-dsDNA complexes, that concomitantly also leads to better unwinding. RAD52 itself being a highly aggregated protein perhaps acts as scaffold to bring together RAD51 and DNA molecules into large co-aggregates of RAD52-RAD51-DNA complexes to promote RAD51 mediated DNA unwinding reaction, when appropriate nucleotide cofactors are available, presumably through macromolecular crowding effects. Our work highlights the functional link between aggregation of protein-DNA comple...Continue Reading

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Citations

Aug 19, 2011·Cancer Immunology, Immunotherapy : CII·Gregory LeeSuzanne Potzold
Feb 14, 2013·Pathology Oncology Research : POR·Agnieszka SassiKatarzyna Wozniak
May 17, 2013·Journal of Biochemistry·Shalini Verma, Basuthkar J Rao
Feb 19, 2014·Parasite : Journal De La Société Française De Parasitologie·Ma del Socorro Charcas-LopezLaurence A Marchat

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Methods Mentioned

BETA
immunoprecipitation
electrophoresis
linear dichroism
gel
Dynamic Light Scattering
Thin

Software Mentioned

Image J

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