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. |
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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 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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