Model of abasic site DNA cross-link repair, from the architecture of NEIL3 DNA binding domains to the X-structure model
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F22%3A00561949" target="_blank" >RIV/61388963:_____/22:00561949 - isvavai.cz</a>
Alternative codes found
RIV/00216208:11310/22:10451255
Result on the web
<a href="https://doi.org/10.1093/nar/gkac793" target="_blank" >https://doi.org/10.1093/nar/gkac793</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1093/nar/gkac793" target="_blank" >10.1093/nar/gkac793</a>
Alternative languages
Result language
angličtina
Original language name
Model of abasic site DNA cross-link repair, from the architecture of NEIL3 DNA binding domains to the X-structure model
Original language description
Covalent DNA interstrand crosslinks are toxic DNA damage lesions that block the replication machinery that can cause a genomic instability. Ubiquitous abasic DNA sites are particularly susceptible to spontaneous cross-linking with a base from the opposite DNA strand. Detection of a crosslink induces the DNA helicase ubiquitination that recruits NEIL3, a DNA glycosylase responsible for the lesion removal. NEIL3 utilizes several zinc finger domains indispensable for its catalytic NEI domain repairing activity. They recruit NEIL3 to the repair site and bind the single-stranded DNA. However, the molecular mechanism underlying their roles in the repair process is unknown. Here, we report the structure of the tandem zinc-finger GRF domain of NEIL3 and reveal the molecular details of its interaction with DNA. Our biochemical data indicate the preferential binding of the GRF domain to the replication fork. In addition, we obtained a structure for the catalytic NEI domain in complex with the DNA reaction intermediate that allowed us to construct and validate a model for the interplay between the NEI and GRF domains in the recognition of an interstrand cross-link. Our results suggest a mechanism for recognition of the DNA replication X-structure by NEIL3, a key step in the interstrand cross-link repair.
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
<a href="/en/project/EF16_019%2F0000729" target="_blank" >EF16_019/0000729: Chemical biology for drugging undruggable targets</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2022
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
50
Issue of the periodical within the volume
18
Country of publishing house
GB - UNITED KINGDOM
Number of pages
13
Pages from-to
10436-10448
UT code for WoS article
000859179700001
EID of the result in the Scopus database
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