Chromatin Immunoprecipitation Reveals p53 Binding to G-Quadruplex DNA Sequences in Myeloid Leukemia Cell Lines
Clarifying functions of the p53 protein is a crucial aspect of cancer research. We analyzed the binding sites of p53 wild-type (WT) protein and its oncologically significant mutants and evaluated their transactivation properties using a functional yeast assay. Unlike the binding sites as determined in myeloid leukemia cell lines by chromatin immunoprecipitation of p53-R175H, p53-Y220C, p53-M237I, p53-R248Q, and p53-R273H mutants, the target sites of p53-WT and p53-R282W were significantly associated with putative G-quadruplex sequences (PQSs). Guanine-quadruplex (G-quadruplex or G4) formation in these sequences was evaluated by using a set of biophysical methods. G4s can modulate gene expression induced by p53. At low p53 expression level, PQS upstream of the p53-response element (RE) leads to greater gene expression induced by p53-R282W compared to that for the RE without PQS. Meanwhile, p53-WT protein expression is decreased by the PQS presence. At a high p53 expression level, the presence of PQS leads to a decreased expression of the reporter regardless of the distance and localization of the G4 from the RE.
Authors
- Michaela Dobrovolná (ORCID: https://orcid.org/0000-0002-4979-0387)
- Natália Valková (ORCID: https://orcid.org/0000-0003-3898-7229)
- Václav Brázda (ORCID: https://orcid.org/0000-0003-2837-4226)
- Pedro A. Sánchez‐Murcia (ORCID: https://orcid.org/0000-0001-8415-870X)
- Libuše Kratochvilová
- Alessandra Dinová
Institutions
- Czech Academy of Sciences, Institute of Biophysics (CZ)
- BioTechMed-Graz (AT)
- Brno University of Technology (CZ)
Publication Details
- Journal
- ACS Bio & Med Chem Au
- Published
- 2025-02-12
- DOI
- https://doi.org/10.1021/acsbiomedchemau.4c00124
- Citations
- 3
- Primary Topic
- DNA and Nucleic Acid Chemistry
- Type
- article
- Field-Weighted Citation Impact
- 2.42
Funders
- Grantová Agentura České Republiky
- Akademie Věd České Republiky
- Karl-Franzens-Universität Graz
- Medizinische Universität Graz