p53 binds human telomeric G-quadruplex in vitro

Result code in IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68081707%3A_____%2F16%3A00471957" target="_blank" >RIV/68081707:_____/16:00471957 - isvavai.cz</a>

Result on the web

<a href="http://dx.doi.org/10.1016/j.biochi.2016.07.004" target="_blank" >http://dx.doi.org/10.1016/j.biochi.2016.07.004</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.biochi.2016.07.004" target="_blank" >10.1016/j.biochi.2016.07.004</a>

Result language

angličtina

Original language name

p53 binds human telomeric G-quadruplex in vitro

Original language description

The tumor suppressor protein p53 is a key factor in genome stability and one of the most studied of DNA binding proteins. This is the first study on the interaction of wild-type p53 with guanine quadruplexes formed by the human telomere sequence. Using electromobility shift assay and ELISA, we show that p53 binding to telomeric G-quadruplexes increases with the number of telomeric repeats. Further, p53 strongly favors G-quadruplexes folded in potassium over those formed in sodium, thus indicating the telomeric G-quadruplex conformational selectivity of p53. The presence of the quadruplex-stabilizing ligand, N-methyl mesoporphyrin IX (NMM), increases p53 recognition of G-quadruplexes in potassium. Using deletion mutants and selective p53 core domain oxidation, both p53 DNA binding domains are shown to be crucial for telomeric G-quadruplex recognition. (C) 2016 Elsevier B.V. and Societe Francaise de Biochimie et Biologie Moleculaire (SFBBM). All rights reserved.

Czech name

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Czech description

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Type

J_x - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)

CEP classification

BO - Biophysics

OECD FORD branch

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Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Publication year

2016

Confidentiality

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

Name of the periodical

Biochimie

ISSN

0300-9084

e-ISSN

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Volume of the periodical

128

Issue of the periodical within the volume

SEPT2016

Country of publishing house

FR - FRANCE

Number of pages

9

Pages from-to

83-91

UT code for WoS article

000385327700009

EID of the result in the Scopus database

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