RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F19%3A00518318" target="_blank" >RIV/68081707:_____/19:00518318 - isvavai.cz</a>
Alternative codes found
RIV/61989592:15310/19:73597603
Result on the web
<a href="https://www.nature.com/articles/s41467-019-11900-8.pdf" target="_blank" >https://www.nature.com/articles/s41467-019-11900-8.pdf</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1038/s41467-019-11900-8" target="_blank" >10.1038/s41467-019-11900-8</a>
Alternative languages
Result language
angličtina
Original language name
RuvC uses dynamic probing of the Holliday junction to achieve sequence specificity and efficient resolution
Original language description
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.
Czech name
—
Czech description
—
Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
—
OECD FORD branch
10403 - Physical chemistry
Result continuities
Project
<a href="/en/project/EF15_003%2F0000477" target="_blank" >EF15_003/0000477: Structural gymnastics of nucleic acids: from molecular principles through biological functions to therapeutic targets.</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nature Communications
ISSN
2041-1723
e-ISSN
—
Volume of the periodical
10
Issue of the periodical within the volume
SEP 10 2019
Country of publishing house
GB - UNITED KINGDOM
Number of pages
10
Pages from-to
4102
UT code for WoS article
000484992500001
EID of the result in the Scopus database
—