Interaction of p53 proteins with G-quadruplexes

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F62157124%3A16370%2F19%3A43878279" target="_blank" >RIV/62157124:16370/19:43878279 - isvavai.cz</a>
Result on the web
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DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Interaction of p53 proteins with G-quadruplexes
Original language description
Tumor suppressor p53 is a key transcriptional regulator of genes involved in mechanisms including DNA damage response, cell cycle arrest or apoptosis. Function of p53 depends on its ability to recognize response elements in the genome, which may also form diverse non-B DNA structures. Our results show that wild-type p53 binds to parallel MYC promoter G-quadruplex with affinity comparable to p53 consensus sequence and that the C-terminal region of p53 (aa 320-393) is important for G-quadruplex recognition. Binding of p53 to G-quadruplexes formed by human telomeric repeats is dependent on the presence of potassium or sodium cations and p53 binding is further enhanced after annealing of the G-quadruplexes with G-quadruplex ligand NMM. We propose that G-quadruplexes have a role as recognition elements in p53-dependent gene regulation.
Czech name
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Czech description
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Publication year
2019
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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