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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

  • Czech description

Classification

  • Type

    J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database

  • CEP classification

  • 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