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FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA

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    SYSNO ASEP0556576
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleFOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA
    Author(s) Mandal, R. (CZ)
    Kohoutová, Klára (FGU-C) ORCID
    Petrvalská, Olivia (FGU-C) RID, ORCID, SAI
    Horváth, M. (CZ)
    Srb, Pavel (UOCHB-X) RID, ORCID
    Veverka, Václav (UOCHB-X) RID, ORCID
    Obšilová, Veronika (FGU-C) RID, ORCID, SAI
    Obšil, Tomáš (FGU-C) RID, ORCID
    Article numbere4287
    Source TitleProtein Science. - : Wiley - ISSN 0961-8368
    Roč. 31, č. 5 (2022)
    Number of pages13 s.
    Languageeng - English
    CountryUS - United States
    KeywordsDNA binding ; forkhead box O 4 ; nuclear magnetic resonance ; protein-protein interaction ; senescence ; transcription factor p53
    OECD categoryBiochemistry and molecular biology
    R&D ProjectsGA21-02080S GA ČR - Czech Science Foundation (CSF)
    Research InfrastructureCIISB II - 90127 - Masarykova univerzita
    Method of publishingLimited access
    Institutional supportFGU-C - RVO:67985823 ; UOCHB-X - RVO:61388963
    UT WOS000788245500005
    EID SCOPUS85129098228
    DOI10.1002/pro.4287
    AnnotationTranscription factor p53 protects cells against tumorigenesis when subjected to various cellular stresses. Under these conditions, p53 interacts with transcription factor Forkhead box O (FOXO) 4, thereby inducing cellular senescence by upregulating the transcription of senescence-associated protein p21. However, the structural details of this interaction remain unclear. Here, we characterize the interaction between p53 and FOXO4 by NMR, chemical cross-linking, and analytical ultracentrifugation. Our results reveal that the interaction between p53 TAD and the FOXO4 Forkhead domain is essential for the overall stability of the p53:FOXO4 complex. Furthermore, contacts involving the N-terminal segment of FOXO4, the C-terminal negative regulatory domain of p53 and the DNA-binding domains of both proteins stabilize the complex, whose formation blocks p53 binding to DNA but without affecting the DNA-binding properties of FOXO4. Therefore, our structural findings may help to understand the intertwined functions of p53 and FOXO4 in cellular homeostasis, longevity, and stress response.
    WorkplaceInstitute of Physiology
    ContactLucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
    Year of Publishing2023
    Electronic addresshttps://doi.org/10.1002/pro.4287
Number of the records: 1  

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