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@article{2262447,
author = {Mandal, Raju and Kohoutova, Klara and Petrvalska, Olivia and Horvath, Matej and Srb, Pavel and Veverka, Vaclav and Obsilova, Veronika and Obsil, Tomas},
article_location = {HOBOKEN},
article_number = {5},
doi = {http://dx.doi.org/10.1002/pro.4287},
keywords = {DNA binding; Forkhead box O 4; nuclear magnetic resonance; protein-protein interaction; senescence; transcription factor p53},
language = {eng},
issn = {0961-8368},
journal = {Protein Science},
title = {FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA},
url = {https://onlinelibrary.wiley.com/doi/10.1002/pro.4287},
volume = {31},
year = {2022}
}
TY - JOUR
ID - 2262447
AU - Mandal, Raju - Kohoutova, Klara - Petrvalska, Olivia - Horvath, Matej - Srb, Pavel - Veverka, Vaclav - Obsilova, Veronika - Obsil, Tomas
PY - 2022
TI - FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA
JF - Protein Science
VL - 31
IS - 5
SP - 1-13
EP - 1-13
PB - JOHN WILEY & SONS INC
SN - 09618368
KW - DNA binding
KW - Forkhead box O 4
KW - nuclear magnetic resonance
KW - protein-protein interaction
KW - senescence
KW - transcription factor p53
UR - https://onlinelibrary.wiley.com/doi/10.1002/pro.4287
N2 - Transcription 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.
ER -
MANDAL, Raju, Klara KOHOUTOVA, Olivia PETRVALSKA, Matej HORVATH, Pavel SRB, Vaclav VEVERKA, Veronika OBSILOVA a Tomas OBSIL. FOXO4 interacts with p53 TAD and CRD and inhibits its binding to DNA. \textit{Protein Science}. HOBOKEN: JOHN WILEY \&{}amp; SONS INC, 2022, roč.~31, č.~5, s.~1-13. ISSN~0961-8368. Dostupné z: https://dx.doi.org/10.1002/pro.4287.
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