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@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 a Simon J. BOULTON. A Polar and Nucleotide-Dependent Mechanism of Action for RAD51 Paralogs in RAD51 Filament Remodeling. \textit{Molecular Cell}. Cambridge: Cell Press, roč.~64, č.~5, s.~926-939. ISSN~1097-2765. doi:10.1016/j.molcel.2016.10.020. 2016.
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