p53 binds human telomeric G-quadruplex in vitro

J 2016

p53 binds human telomeric G-quadruplex in vitro

ADÁMIK, Matej; Iva KEJNOVSKÁ; Pavla BAŽANTOVÁ; Marek PETR; Daniel RENČIUK et al.

Základní údaje

Originální název

p53 binds human telomeric G-quadruplex in vitro

Autoři

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

Vydání

Biochimie, Paris, Elsevier France- editions Scientifiques Medicales Elsevier, 2016, 0300-9084

Další údaje

Jazyk

angličtina

Typ výsledku

Článek v odborném periodiku

Utajení

není předmětem státního či obchodního tajemství

Odkazy

URL

Impakt faktor

Impact factor: 3.112

Označené pro přenos do RIV

Klíčová slova anglicky

G-quadruplex; p53 protein; Telomere DNA; DNA-protein interaction

Příznaky

Mezinárodní význam, Recenzováno

Změněno: 27. 1. 2017 14:56, Mgr. Matej Adámik, Ph.D.

Anotace

V originále

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.

Citovat

ADÁMIK, Matej; Iva KEJNOVSKÁ; Pavla BAŽANTOVÁ; Marek PETR; Daniel RENČIUK; Michaela VORLÍČKOVÁ; Marie BRÁZDOVÁ a Monika ŠVARCOVÁ. p53 binds human telomeric G-quadruplex in vitro. Biochimie. Paris: Elsevier France- editions Scientifiques Medicales Elsevier, 2016, roč. 128, s. 83-91. ISSN 0300-9084. Dostupné z: https://doi.org/10.1016/j.biochi.2016.07.004.

@article{1369966,
   author = {Adámik, Matej and Kejnovská, Iva and Bažantová, Pavla and Petr, Marek and Renčiuk, Daniel and Vorlíčková, Michaela and Brázdová, Marie and Švarcová, Monika},
   article_location = {Paris},
   doi = {https://doi.org/10.1016/j.biochi.2016.07.004},
   keywords = {G-quadruplex; p53 protein; Telomere DNA; DNA-protein interaction},
   language = {eng},
   issn = {0300-9084},
   journal = {Biochimie},
   title = {p53 binds human telomeric G-quadruplex in vitro},
   url = {http://dx.doi.org/10.1016/j.biochi.2016.07.004},
   volume = {128},
   year = {2016}
}

TY  - JOUR
ID  - 1369966
AU  - Adámik, Matej - Kejnovská, Iva - Bažantová, Pavla - Petr, Marek - Renčiuk, Daniel - Vorlíčková, Michaela - Brázdová, Marie - Švarcová, Monika
PY  - 2016
TI  - p53 binds human telomeric G-quadruplex in vitro
JF  - Biochimie
VL  - 128
SP  - 83-91
EP  - 83-91
PB  - Elsevier France- editions Scientifiques Medicales Elsevier
SN  - 03009084
KW  - G-quadruplex
KW  - p53 protein
KW  - Telomere DNA
KW  - DNA-protein interaction
UR  - http://dx.doi.org/10.1016/j.biochi.2016.07.004
L2  - http://dx.doi.org/10.1016/j.biochi.2016.07.004
N2  - 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.
ER  -

ADÁMIK, Matej; Iva KEJNOVSKÁ; Pavla BAŽANTOVÁ; Marek PETR; Daniel RENČIUK; Michaela VORLÍČKOVÁ; Marie BRÁZDOVÁ a Monika ŠVARCOVÁ. p53 binds human telomeric G-quadruplex in vitro. \textit{Biochimie}. Paris: Elsevier France- editions Scientifiques Medicales Elsevier, 2016, roč.~128, s.~83-91. ISSN~0300-9084. Dostupné z: https://doi.org/10.1016/j.biochi.2016.07.004.

Přehled o publikaci