Detail
Článek
Článek online
FT
Medvik - BMČ
  • Je něco špatně v tomto záznamu ?

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

M. Špírek, MRG. Taylor, O. Belan, SJ. Boulton, L. Krejci

. 2021 ; 12 (1) : 5545. [pub] 20210920

Jazyk angličtina Země Velká Británie

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc22003700

Grantová podpora
Wellcome Trust - United Kingdom
110014/Z/15/Z Wellcome Trust - United Kingdom
206292/E/17/Z Wellcome Trust - United Kingdom

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.

Citace poskytuje Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc22003700
003      
CZ-PrNML
005      
20220127145950.0
007      
ta
008      
220113s2021 xxk f 000 0|eng||
009      
AR
024    7_
$a 10.1038/s41467-021-25830-x $2 doi
035    __
$a (PubMed)34545070
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxk
100    1_
$a Špírek, Mário $u International Clinical Research Center, St. Anne's University Hospital in Brno, 62500, Brno, Czech Republic $u Department of Biology Masaryk University, 62500, Brno, Czech Republic
245    10
$a Nucleotide proofreading functions by nematode RAD51 paralogs facilitate optimal RAD51 filament function / $c M. Špírek, MRG. Taylor, O. Belan, SJ. Boulton, L. Krejci
520    9_
$a 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.
650    _2
$a adenosindifosfát $x farmakologie $7 D000244
650    _2
$a adenosintrifosfát $x farmakologie $7 D000255
650    _2
$a zvířata $7 D000818
650    _2
$a Caenorhabditis elegans $x metabolismus $7 D017173
650    _2
$a proteiny Caenorhabditis elegans $x metabolismus $7 D029742
650    _2
$a jednovláknová DNA $x metabolismus $7 D004277
650    _2
$a fluorescence $7 D005453
650    _2
$a interferometrie $7 D007368
650    _2
$a nukleotidy $x metabolismus $7 D009711
650    _2
$a vazba proteinů $x účinky léků $7 D011485
650    _2
$a stabilita proteinů $x účinky léků $7 D055550
650    _2
$a rekombinasa Rad51 $x chemie $x metabolismus $7 D051135
650    12
$a sekvenční homologie aminokyselin $7 D017386
650    _2
$a druhová specificita $7 D013045
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Taylor, Martin R G $u The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK
700    1_
$a Belan, Ondrej $u The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK $u National Centre for Biomolecular Research, Masaryk University, 62500, Brno, Czech Republic
700    1_
$a Boulton, Simon J $u The Francis Crick Institute, 1 Midland Road, London, NW1 1AT, UK
700    1_
$a Krejci, Lumir $u International Clinical Research Center, St. Anne's University Hospital in Brno, 62500, Brno, Czech Republic. lkrejci@chemi.muni.cz $u Department of Biology Masaryk University, 62500, Brno, Czech Republic. lkrejci@chemi.muni.cz $u National Centre for Biomolecular Research, Masaryk University, 62500, Brno, Czech Republic. lkrejci@chemi.muni.cz
773    0_
$w MED00184850 $t Nature communications $x 2041-1723 $g Roč. 12, č. 1 (2021), s. 5545
856    41
$u https://pubmed.ncbi.nlm.nih.gov/34545070 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y p $z 0
990    __
$a 20220113 $b ABA008
991    __
$a 20220127145946 $b ABA008
999    __
$a ok $b bmc $g 1751222 $s 1154849
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2021 $b 12 $c 1 $d 5545 $e 20210920 $i 2041-1723 $m Nature communications $n Nat Commun $x MED00184850
GRA    __
$p Wellcome Trust $2 United Kingdom
GRA    __
$a 110014/Z/15/Z $p Wellcome Trust $2 United Kingdom
GRA    __
$a 206292/E/17/Z $p Wellcome Trust $2 United Kingdom
LZP    __
$a Pubmed-20220113

Najít záznam

Citační ukazatele

Možnosti archivace