Characterization of the interaction between the tumour suppressor p53 and heme and its role in the protein conformational dynamics studied by various spectroscopic techniques and hydrogen/deuterium exchange coupled with mass spectrometry
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378271%3A_____%2F23%3A00579255" target="_blank" >RIV/68378271:_____/23:00579255 - isvavai.cz</a>
Alternative codes found
RIV/86652052:_____/23:N0000024 RIV/00216208:11310/23:10464446
Result on the web
<a href="https://doi.org/10.1016/j.jinorgbio.2023.112180" target="_blank" >https://doi.org/10.1016/j.jinorgbio.2023.112180</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.jinorgbio.2023.112180" target="_blank" >10.1016/j.jinorgbio.2023.112180</a>
Alternative languages
Result language
angličtina
Original language name
Characterization of the interaction between the tumour suppressor p53 and heme and its role in the protein conformational dynamics studied by various spectroscopic techniques and hydrogen/deuterium exchange coupled with mass spectrometry
Original language description
The tumour suppressor p53 regulates the expression of a myriad of proteins that are important for numerous cellular processes. Aside from DNA, p53 can interact with many types of partners including proteins and small organic molecules. In this study, we used various spectroscopic studies to conduct a thorough biophysical characterization of the interaction between p53 and heme concerning the oxidation, spin, coordination, and ligand state of heme iron. We found that the p53 oligomeric state and zinc biding ability are preserved upon the interaction with heme. Moreover, we described the effect of heme binding on the conformational dynamics of p53 by hydrogen/deuterium exchange coupled with mass spectrometry. Specifically, the conformational flexibility of p53 is significantly increased upon interaction with heme, while its affinity to a specific DNA sequence is reduced by heme. The inhibitory effect of DNA binding by heme is partially reversible.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10402 - Inorganic and nuclear chemistry
Result continuities
Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2023
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
Journal of Inorganic Biochemistry
ISSN
0162-0134
e-ISSN
1873-3344
Volume of the periodical
243
Issue of the periodical within the volume
June
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
14
Pages from-to
112180
UT code for WoS article
000957264000001
EID of the result in the Scopus database
2-s2.0-85150193031