Number of the records: 1  

p53 binds human telomeric G-quadruplex in vitro

  1. 1.
    SYSNO ASEP0471957
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    Titlep53 binds human telomeric G-quadruplex in vitro
    Author(s) Adámik, Matěj (BFU-R) ORCID
    Kejnovská, Iva (BFU-R) RID, ORCID
    Bažantová, Pavla (BFU-R)
    Petr, Marek (BFU-R) ORCID
    Renčiuk, Daniel (BFU-R) RID, ORCID
    Vorlíčková, Michaela (BFU-R) RID, ORCID
    Brázdová, Marie (BFU-R) RID, ORCID
    Number of authors7
    Source TitleBiochimie. - : Elsevier - ISSN 0300-9084
    Roč. 128, SEPT2016 (2016), s. 83-91
    Number of pages9 s.
    Publication formPrint - P
    Languageeng - English
    CountryFR - France
    Keywordscrystal-structure ; human-chromosomes ; supercoiled dna
    Subject RIVBO - Biophysics
    R&D ProjectsGA13-36108S GA ČR - Czech Science Foundation (CSF)
    GP14-33947P GA ČR - Czech Science Foundation (CSF)
    Institutional supportBFU-R - RVO:68081707
    UT WOS000385327700009
    DOI10.1016/j.biochi.2016.07.004
    AnnotationThe 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.
    WorkplaceInstitute of Biophysics
    ContactJana Poláková, polakova@ibp.cz, Tel.: 541 517 244
    Year of Publishing2017
Number of the records: 1  

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