Nucleotide proofreading functions by nematode RAD51 paralogs
facilitate optimal RAD51 filament function

J 2021

Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function

ŠPÍREK, Mário, M. R. G. TAYLOR, Ondrej BELÁŇ, S. J. BOULTON, Lumír KREJČÍ et. al.

Základní údaje

Originální název

Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function

Autoři

ŠPÍREK, Mário (703 Slovensko, domácí), M. R. G. TAYLOR, Ondrej BELÁŇ (703 Slovensko, domácí), S. J. BOULTON a Lumír KREJČÍ (203 Česká republika, garant, domácí)

Vydání

Nature Communications, London, Nature Publishing Group, 2021, 2041-1723

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Obor

10608 Biochemistry and molecular biology

Stát vydavatele

Německo

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 17.694

Kód RIV

RIV/00216224:14110/21:00119274

Organizační jednotka

Lékařská fakulta

DOI

http://dx.doi.org/10.1038/s41467-021-25830-x

UT WoS

000698606100024

Klíčová slova anglicky

RAD51; nucleotide proofreading functions

Štítky

14110513, podil, rivok

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 30. 11. 2022 13:33, Mgr. Tereza Miškechová

Anotace

V originále

The RAD51 recombinase assembles as helical nucleoprotein filaments on single-stranded DNA (ssDNA) and mediates invasion and strand exchange with homologous duplex DNA (dsDNA) during homologous recombination (HR), as well as protection and restart of stalled replication forks. Strand invasion by RAD51-ssDNA complexes depends on ATP binding. However, RAD51 can bind ssDNA in non-productive ADP-bound or nucleotide-free states, and ATP-RAD51-ssDNA complexes hydrolyse ATP over time. Here, we define unappreciated mechanisms by which the RAD51 paralog complex RFS-1/RIP-1 limits the accumulation of RAD-51-ssDNA complexes with unfavorable nucleotide content. We find RAD51 paralogs promote the turnover of ADP-bound RAD-51 from ssDNA, in striking contrast to their ability to stabilize productive ATP-bound RAD-51 nucleoprotein filaments. In addition, RFS-1/RIP-1 inhibits binding of nucleotide-free RAD-51 to ssDNA. We propose that 'nucleotide proofreading' activities of RAD51 paralogs co-operate to ensure the enrichment of active, ATP-bound RAD-51 filaments on ssDNA to promote HR. A RAD51 paralog complex, RFS-1/RIP-1, is shown to control ssDNA binding and dissociation by RAD-51 differentially in the presence and absence of nucleotide cofactors. These nucleotide proofreading activities drive a preferential accumulation of RAD-51-ssDNA complexes with optimal nucleotide content.

Návaznosti

EF16_025/0007381, projekt VaV

Název: Preklinická progrese nových organických sloučenin s cílenou biologickou aktivitou

GX21-22593X, projekt VaV

Název: Identifikace a charakterizace proteinů zahrnutých v metabolismu G-kvadruplexů a R-smyček a jejich vztah k replikaci DNA

MUNI/G/1594/2019, interní kód MU

Název: RecQ4 – a protein hub required for proper replication and recombination and its implications in Rothmund-Thomson Syndrome

Investor: Masarykova univerzita, RecQ4 – a protein hub required for proper replication and recombination and its implications in Rothmund-Thomson Syndrome, INTERDISCIPLINARY - Mezioborové výzkumné projekty

206292/E/17/Z, interní kód MU

Název: Mechanics and execution of homologous recombination - biophysics to the organism

Investor: Wellcome Trust, Mechanics and execution of homologous recombination - biophysics to the organism

Citovat

ŠPÍREK, Mário, M. R. G. TAYLOR, Ondrej BELÁŇ, S. J. BOULTON a Lumír KREJČÍ. Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function. Nature Communications. London: Nature Publishing Group, 2021, roč. 12, č. 1, s. 1-12. ISSN 2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-021-25830-x.

@article{1798275,
   author = {Špírek, Mário and Taylor, M. R. G. and Beláň, Ondrej and Boulton, S. J. and Krejčí, Lumír},
   article_location = {London},
   article_number = {1},
   doi = {http://dx.doi.org/10.1038/s41467-021-25830-x},
   keywords = {RAD51; nucleotide proofreading functions},
   language = {eng},
   issn = {2041-1723},
   journal = {Nature Communications},
   title = {Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function},
   url = {https://www.nature.com/articles/s41467-021-25830-x},
   volume = {12},
   year = {2021}
}

TY  - JOUR
ID  - 1798275
AU  - Špírek, Mário - Taylor, M. R. G. - Beláň, Ondrej - Boulton, S. J. - Krejčí, Lumír
PY  - 2021
TI  - Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function
JF  - Nature Communications
VL  - 12
IS  - 1
SP  - 1-12
EP  - 1-12
PB  - Nature Publishing Group
SN  - 20411723
KW  - RAD51
KW  - nucleotide proofreading functions
UR  - https://www.nature.com/articles/s41467-021-25830-x
N2  - The RAD51 recombinase assembles as helical nucleoprotein filaments on single-stranded DNA (ssDNA) and mediates invasion and strand exchange with homologous duplex DNA (dsDNA) during homologous recombination (HR), as well as protection and restart of stalled replication forks. Strand invasion by RAD51-ssDNA complexes depends on ATP binding. However, RAD51 can bind ssDNA in non-productive ADP-bound or nucleotide-free states, and ATP-RAD51-ssDNA complexes hydrolyse ATP over time. Here, we define unappreciated mechanisms by which the RAD51 paralog complex RFS-1/RIP-1 limits the accumulation of RAD-51-ssDNA complexes with unfavorable nucleotide content. We find RAD51 paralogs promote the turnover of ADP-bound RAD-51 from ssDNA, in striking contrast to their ability to stabilize productive ATP-bound RAD-51 nucleoprotein filaments. In addition, RFS-1/RIP-1 inhibits binding of nucleotide-free RAD-51 to ssDNA. We propose that 'nucleotide proofreading' activities of RAD51 paralogs co-operate to ensure the enrichment of active, ATP-bound RAD-51 filaments on ssDNA to promote HR. A RAD51 paralog complex, RFS-1/RIP-1, is shown to control ssDNA binding and dissociation by RAD-51 differentially in the presence and absence of nucleotide cofactors. These nucleotide proofreading activities drive a preferential accumulation of RAD-51-ssDNA complexes with optimal nucleotide content.
ER  -

ŠPÍREK, Mário, M. R. G. TAYLOR, Ondrej BELÁŇ, S. J. BOULTON a Lumír KREJČÍ. Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function. \textit{Nature Communications}. London: Nature Publishing Group, 2021, roč.~12, č.~1, s.~1-12. ISSN~2041-1723. Dostupné z: https://dx.doi.org/10.1038/s41467-021-25830-x.

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