Single-molecule visualization of human RECQ5 interactions with single-stranded DNA recombination intermediates
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14110%2F21%3A00118917" target="_blank" >RIV/00216224:14110/21:00118917 - isvavai.cz</a>
Alternative codes found
RIV/00159816:_____/21:00075161
Result on the web
<a href="https://academic.oup.com/nar/article/49/1/285/6041011" target="_blank" >https://academic.oup.com/nar/article/49/1/285/6041011</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkaa1184" target="_blank" >10.1093/nar/gkaa1184</a>
Alternative languages
Result language
angličtina
Original language name
Single-molecule visualization of human RECQ5 interactions with single-stranded DNA recombination intermediates
Original language description
RECQ5 is one of five RecQ helicases found in humans and is thought to participate in homologous DNA recombination by acting as a negative regulator of the recombinase protein RAD51. Here, we use kinetic and single molecule imaging methods to monitor RECQ5 behavior on various nucleoprotein complexes. Our data demonstrate that RECQ5 can act as an ATP-dependent single-stranded DNA (ssDNA) motor protein and can translocate on ssDNA that is bound by replication protein A (RPA). RECQ5 can also translocate on RAD51-coated ssDNA and readily dismantles RAD51-ssDNA filaments. RECQ5 interacts with RAD51 through protein-protein contacts, and disruption of this interface through a RECQ5-F666A mutation reduces translocation velocity by similar to 50%. However, RECQ5 readily removes the ATP hydrolysis-deficient mutant RAD51-K133R from ssDNA, suggesting that filament disruption is not coupled to the RAD51 ATP hydrolysis cycle. RECQ5 also readily removes RAD51-I287T, a RAD51 mutant with enhanced ssDNA-binding activity, from ssDNA. Surprisingly, RECQ5 can bind to double-stranded DNA (dsDNA), but it is unable to translocate. Similarly, RECQ5 cannot dismantle RAD51-bound heteroduplex joint molecules. Our results suggest that the roles of RECQ5 in genome maintenance may be regulated in part at the level of substrate specificity.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10608 - Biochemistry and molecular biology
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)
Others
Publication year
2021
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Nucleic acids research
ISSN
0305-1048
e-ISSN
1362-4962
Volume of the periodical
49
Issue of the periodical within the volume
1
Country of publishing house
GB - UNITED KINGDOM
Number of pages
21
Pages from-to
285-305
UT code for WoS article
000610552100027
EID of the result in the Scopus database
2-s2.0-85099721998