Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F17%3A00095119" target="_blank" >RIV/00216224:14740/17:00095119 - isvavai.cz</a>

Result on the web

<a href="https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkx812" target="_blank" >https://academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkx812</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1093/nar/gkx812" target="_blank" >10.1093/nar/gkx812</a>

Result language

angličtina

Original language name

Basic domain of telomere guardian TRF2 reduces D-loop unwinding whereas Rap1 restores it

Original language description

Telomeric repeat binding factor 2 (TRF2) folds human telomeres into loops to prevent unwanted DNA repair and chromosome end-joining. The N-terminal basic domain of TRF2 (B-domain) protects the telomeric displacement loop (D-loop) from cleavage by endonucleases. Repressor activator protein 1 (Rap1) binds TRF2 and improves telomeric DNA recognition. We found that the B-domain of TRF2 stabilized the D-loop and thus reduced unwinding by BLM and RPA, whereas the formation of the Rap1–TRF2 complex restored DNA unwinding. To understand how the B-domain of TRF2 affects DNA binding and D-loop processing, we analyzed DNA binding of full-length TRF2 and a truncated TRF2 construct lacking the B-domain. We quantified how the B-domain improves TRF2’s interaction with DNA via enhanced long-range electrostatic interactions. We developed a structural envelope model of the B-domain bound on DNA. The model revealed that the B-domain is flexible in solution but becomes rigid upon binding to telomeric DNA. We proposed a mechanism for how the B-domain stabilizes the D-loop.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10610 - Biophysics

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)

Publication year

2017

Confidentiality

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Name of the periodical

Nucleic Acids Research

ISSN

0305-1048

e-ISSN

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Volume of the periodical

45

Issue of the periodical within the volume

21

Country of publishing house

GB - UNITED KINGDOM

Number of pages

11

Pages from-to

12170-12180

UT code for WoS article

000417691300016

EID of the result in the Scopus database

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