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

J 2016

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

TAYLOR, Martin R.G., Mário ŠPÍREK, Chu Jian MA, Raffaella CARZANIGA, Tohru TAKAKI et. al.

Basic information

Original name

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

Authors

TAYLOR, Martin R.G. (826 United Kingdom of Great Britain and Northern Ireland), Mário ŠPÍREK (703 Slovakia, belonging to the institution), Chu Jian MA (840 United States of America), Raffaella CARZANIGA (826 United Kingdom of Great Britain and Northern Ireland), Tohru TAKAKI (826 United Kingdom of Great Britain and Northern Ireland), Lucy M. COLLINSON (826 United Kingdom of Great Britain and Northern Ireland), Eric C. GREENE (840 United States of America), Lumír KREJČÍ (203 Czech Republic, guarantor, belonging to the institution) and Simon J. BOULTON (826 United Kingdom of Great Britain and Northern Ireland)

Edition

Molecular Cell, Cambridge, Cell Press, 2016, 1097-2765

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

Genetics and molecular biology

Country of publisher

United Kingdom of Great Britain and Northern Ireland

Confidentiality degree

není předmětem státního či obchodního tajemství

Impact factor

Impact factor: 14.714

RIV identification code

RIV/00216224:14110/16:00088541

Organization unit

Faculty of Medicine

DOI

http://dx.doi.org/10.1016/j.molcel.2016.10.020

UT WoS

000389515500009

Keywords in English

SINGLE-STRANDED-DNA; INDUCED FLUORESCENCE ENHANCEMENT; CANCER TUMOR-SUPPRESSOR; REPLICATION PROTEIN-A; HOMOLOGOUS RECOMBINATION; SACCHAROMYCES-CEREVISIAE; MAMMALIAN-CELLS; COMPLEX; REPAIR; PROMOTES

Abstract

V originále

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 50 end of RAD-51-ssDNA filaments. Filament end capping propagates a stabilizing effect with a 5'-> 3' 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.

Links

GAP207/12/2323, research and development project

Name: Endonuleazová a translokázová aktivita v restričních-modifikáčních komplexéch typu I

Investor: Czech Science Foundation

GA13-26629S, research and development project

Name: SUMO a stability genomu

Investor: Czech Science Foundation

Citovat

TAYLOR, Martin R.G., Mário ŠPÍREK, Chu Jian MA, Raffaella CARZANIGA, Tohru TAKAKI, Lucy M. COLLINSON, Eric C. GREENE, Lumír KREJČÍ and Simon J. BOULTON. A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling. Molecular Cell. Cambridge: Cell Press, 2016, vol. 64, No 5, p. 926-939. ISSN 1097-2765. Available from: https://dx.doi.org/10.1016/j.molcel.2016.10.020.

@article{1367405,
   author = {Taylor, Martin R.G. and Špírek, Mário and Ma, Chu Jian and Carzaniga, Raffaella and Takaki, Tohru and Collinson, Lucy M. and Greene, Eric C. and Krejčí, Lumír and Boulton, Simon J.},
   article_location = {Cambridge},
   article_number = {5},
   doi = {http://dx.doi.org/10.1016/j.molcel.2016.10.020},
   keywords = {SINGLE-STRANDED-DNA; INDUCED FLUORESCENCE ENHANCEMENT; CANCER TUMOR-SUPPRESSOR; REPLICATION PROTEIN-A; HOMOLOGOUS RECOMBINATION; SACCHAROMYCES-CEREVISIAE; MAMMALIAN-CELLS; COMPLEX; REPAIR; PROMOTES},
   language = {eng},
   issn = {1097-2765},
   journal = {Molecular Cell},
   title = {A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling},
   volume = {64},
   year = {2016}
}

TY  - JOUR
ID  - 1367405
AU  - Taylor, Martin R.G. - Špírek, Mário - Ma, Chu Jian - Carzaniga, Raffaella - Takaki, Tohru - Collinson, Lucy M. - Greene, Eric C. - Krejčí, Lumír - Boulton, Simon J.
PY  - 2016
TI  - A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling
JF  - Molecular Cell
VL  - 64
IS  - 5
SP  - 926-939
EP  - 926-939
PB  - Cell Press
SN  - 10972765
KW  - SINGLE-STRANDED-DNA
KW  - INDUCED FLUORESCENCE ENHANCEMENT
KW  - CANCER TUMOR-SUPPRESSOR
KW  - REPLICATION PROTEIN-A
KW  - HOMOLOGOUS RECOMBINATION
KW  - SACCHAROMYCES-CEREVISIAE
KW  - MAMMALIAN-CELLS
KW  - COMPLEX
KW  - REPAIR
KW  - PROMOTES
N2  - 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 50 end of RAD-51-ssDNA filaments. Filament end capping propagates a stabilizing effect with a 5'-> 3' 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.
ER  -

TAYLOR, Martin R.G., Mário ŠPÍREK, Chu Jian MA, Raffaella CARZANIGA, Tohru TAKAKI, Lucy M. COLLINSON, Eric C. GREENE, Lumír KREJČÍ and Simon J. BOULTON. A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling. \textit{Molecular Cell}. Cambridge: Cell Press, 2016, vol.~64, No~5, p.~926-939. ISSN~1097-2765. Available from: https://dx.doi.org/10.1016/j.molcel.2016.10.020.

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