Publication details

p53 binds human telomeric G-quadruplex in vitro

Authors

ADÁMIK Matej KEJNOVSKÁ Iva BAŽANTOVÁ Pavla PETR Marek RENČIUK Daniel VORLÍČKOVÁ Michaela BRÁZDOVÁ Marie ŠVARCOVÁ Monika

Year of publication 2016
Type Article in Periodical
Citation
Web http://dx.doi.org/10.1016/j.biochi.2016.07.004
Doi http://dx.doi.org/10.1016/j.biochi.2016.07.004
Keywords G-quadruplex; p53 protein; Telomere DNA; DNA-protein interaction
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.

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