A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00159816%3A_____%2F16%3A00065823" target="_blank" >RIV/00159816:_____/16:00065823 - isvavai.cz</a>

Alternative codes found

RIV/00216224:14110/16:00088541

Result on the web

<a href="http://dx.doi.org/10.1016/j.molcel.2016.10.020" target="_blank" >http://dx.doi.org/10.1016/j.molcel.2016.10.020</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.molcel.2016.10.020" target="_blank" >10.1016/j.molcel.2016.10.020</a>

Result language

angličtina

Original language name

A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling

Original language description

Central to homologous recombination in eukaryotes is the RAD51 recombinase, which forms helical nucleoprotein filaments on single-stranded DNA (ssDNA) and catalyzes strand invasion with homologous duplex DNA. Various regulatory proteins assist this reaction including the RAD51 paralogs. We recently discovered that a RAD51 paralog complex from C. elegans, RFS-1/RIP-1, functions predominantly downstream of filament assembly by binding and remodeling RAD-51-ssDNA filaments to a conformation more proficient for strand exchange. Here, we demonstrate that RFS-1/RIP-1 acts by shutting down RAD-51 dissociation from ssDNA. Using stopped-flow experiments, we show that RFS-1/RIP-1 confers this dramatic stabilization by capping the 5' end of RAD-51-ssDNA filaments. Filament end capping propagates a stabilizing effect with a 5'RIGHTWARDS ARROW3' polarity approximately 40 nucleotides along individual filaments. Finally, we discover that filament capping and stabilization are dependent on nucleotide binding, but not hydrolysis by RFS-1/RIP-1. These data define the mechanism of RAD51 filament remodeling by RAD51 paralogs.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

CE - Biochemistry

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year

2016

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Molecular Cell

ISSN

1097-2765

e-ISSN

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Volume of the periodical

64

Issue of the periodical within the volume

5

Country of publishing house

US - UNITED STATES

Number of pages

13

Pages from-to

926-939

UT code for WoS article

000389515500009

EID of the result in the Scopus database

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