Detail
Article
Online article
FT
Medvik - BMC
  • Something wrong with this record ?

RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution

KM. Górecka, M. Krepl, A. Szlachcic, J. Poznański, J. Šponer, M. Nowotny,

. 2019 ; 10 (1) : 4102. [pub] 20190910

Language English Country Great Britain

Document type Journal Article, Research Support, Non-U.S. Gov't

Persistent link   https://www.medvik.cz/link/bmc19044538

Grant support
Wellcome Trust - United Kingdom

Holliday junctions (HJs) are four-way DNA structures that occur in DNA repair by homologous recombination. Specialized nucleases, termed resolvases, remove (i.e., resolve) HJs. The bacterial protein RuvC is a canonical resolvase that introduces two symmetric cuts into the HJ. For complete resolution of the HJ, the two cuts need to be tightly coordinated. They are also specific for cognate DNA sequences. Using a combination of structural biology, biochemistry, and a computational approach, here we show that correct positioning of the substrate for cleavage requires conformational changes within the bound DNA. These changes involve rare high-energy states with protein-assisted base flipping that are readily accessible for the cognate DNA sequence but not for non-cognate sequences. These conformational changes and the relief of protein-induced structural tension of the DNA facilitate coordination between the two cuts. The unique DNA cleavage mechanism of RuvC demonstrates the importance of high-energy conformational states in nucleic acid readouts.

References provided by Crossref.org

000      
00000naa a2200000 a 4500
001      
bmc19044538
003      
CZ-PrNML
005      
20200113080923.0
007      
ta
008      
200109s2019 xxk f 000 0|eng||
009      
AR
024    7_
$a 10.1038/s41467-019-11900-8 $2 doi
035    __
$a (PubMed)31506434
040    __
$a ABA008 $b cze $d ABA008 $e AACR2
041    0_
$a eng
044    __
$a xxk
100    1_
$a Górecka, Karolina Maria $u Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, 4 Trojdena St., 02-109, Warsaw, Poland.
245    10
$a RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution / $c KM. Górecka, M. Krepl, A. Szlachcic, J. Poznański, J. Šponer, M. Nowotny,
520    9_
$a Holliday junctions (HJs) are four-way DNA structures that occur in DNA repair by homologous recombination. Specialized nucleases, termed resolvases, remove (i.e., resolve) HJs. The bacterial protein RuvC is a canonical resolvase that introduces two symmetric cuts into the HJ. For complete resolution of the HJ, the two cuts need to be tightly coordinated. They are also specific for cognate DNA sequences. Using a combination of structural biology, biochemistry, and a computational approach, here we show that correct positioning of the substrate for cleavage requires conformational changes within the bound DNA. These changes involve rare high-energy states with protein-assisted base flipping that are readily accessible for the cognate DNA sequence but not for non-cognate sequences. These conformational changes and the relief of protein-induced structural tension of the DNA facilitate coordination between the two cuts. The unique DNA cleavage mechanism of RuvC demonstrates the importance of high-energy conformational states in nucleic acid readouts.
650    _2
$a arginin $x chemie $7 D001120
650    _2
$a bakteriální proteiny $x chemie $7 D001426
650    _2
$a párování bází $7 D020029
650    _2
$a sekvence nukleotidů $7 D001483
650    _2
$a biokatalýza $7 D055162
650    _2
$a DNA bakterií $x chemie $x metabolismus $7 D004269
650    _2
$a křížová struktura DNA $x chemie $7 D045566
650    _2
$a simulace molekulární dynamiky $7 D056004
650    _2
$a Thermus thermophilus $x metabolismus $7 D016963
655    _2
$a časopisecké články $7 D016428
655    _2
$a práce podpořená grantem $7 D013485
700    1_
$a Krepl, Miroslav $u Institute of Biophysics of the Czech Academy of Sciences, Kralovopolska 135, 612 65, Brno, Czech Republic. krepl@ibp.cz.
700    1_
$a Szlachcic, Aleksandra $u Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, 4 Trojdena St., 02-109, Warsaw, Poland.
700    1_
$a Poznański, Jarosław $u Institute of Biochemistry and Biophysics Polish Academy of Sciences, 5a Pawinskiego St., 02-106, Warsaw, Poland.
700    1_
$a Šponer, Jiří $u Institute of Biophysics of the Czech Academy of Sciences, Kralovopolska 135, 612 65, Brno, Czech Republic. Regional Centre of Advanced Technologies and Materials, Faculty of Science, Palacky University Olomouc, Slechtitelu 27, 771 46, Olomouc, Czech Republic.
700    1_
$a Nowotny, Marcin $u Laboratory of Protein Structure, International Institute of Molecular and Cell Biology, 4 Trojdena St., 02-109, Warsaw, Poland. mnowotny@iimcb.gov.pl.
773    0_
$w MED00184850 $t Nature communications $x 2041-1723 $g Roč. 10, č. 1 (2019), s. 4102
856    41
$u https://pubmed.ncbi.nlm.nih.gov/31506434 $y Pubmed
910    __
$a ABA008 $b sig $c sign $y a $z 0
990    __
$a 20200109 $b ABA008
991    __
$a 20200113081255 $b ABA008
999    __
$a ok $b bmc $g 1482807 $s 1083211
BAS    __
$a 3
BAS    __
$a PreBMC
BMC    __
$a 2019 $b 10 $c 1 $d 4102 $e 20190910 $i 2041-1723 $m Nature communications $n Nat Commun $x MED00184850
GRA    __
$p Wellcome Trust $2 United Kingdom
LZP    __
$a Pubmed-20200109

Find record

Citation metrics

Archiving options