0471957 - BFÚ 2017 RIV FR eng J - Článek v odborném periodiku
Adámik, Matěj - Kejnovská, Iva - Bažantová, Pavla - Petr, Marek - Renčiuk, Daniel - Vorlíčková, Michaela - Brázdová, Marie
p53 binds human telomeric G-quadruplex in vitro.
Biochimie. Roč. 128, SEPT2016 (2016), s. 83-91. ISSN 0300-9084. E-ISSN 1638-6183
Grant CEP: GA ČR GA13-36108S; GA ČR(CZ) GP14-33947P
Institucionální podpora: RVO:68081707
Klíčová slova: crystal-structure * human-chromosomes * supercoiled dna
Kód oboru RIV: BO - Biofyzika
Impakt faktor: 3.112, rok: 2016
DOI: https://doi.org/10.1016/j.biochi.2016.07.004

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.

Trvalý link: http://hdl.handle.net/11104/0269318