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Yeast As a Chassis for Developing Functional Assays to Study Human P53
14:57

Yeast As a Chassis for Developing Functional Assays to Study Human P53

Published on: August 4, 2019

P53 forms tight complexes with tms1 of fission yeast

P Wagner

    International Journal of Oncology
    |May 14, 2011
    PubMed

    Insights

    The tms1 protein directly interacts with the tumor suppressor p53 protein. This interaction was confirmed in yeast cells and mapped to the C-terminus of p53.

    Area of Science:

    • Molecular Biology
    • Yeast Genetics
    • Tumor Suppressor Research

    Background:

    • tms1 was identified as a suppressor of p53 mutant-induced growth arrest in fission yeast.
    • tms1 encodes a putative dehydrogenase enzyme.
    • The human p53 protein is a critical tumor suppressor involved in cell cycle control.

    Purpose of the Study:

    • To investigate the direct interaction between tms1 and p53 proteins.
    • To map the specific region of p53 involved in the interaction with tms1.

    Main Methods:

    • Coprecipitation assays using p53- and tms1-specific antibodies in transformed yeast cells.
    • In vitro complex formation assays with purified recombinant p53 C-terminal peptides and tms1 protein.
    • West-Western blot and HPLC analysis for interaction mapping.

    Main Results:

    • Direct physical interaction between tms1 and both wild-type and mutant p53 was demonstrated in vivo.
    • Specific complex formation between recombinant tms1 and p53 C-terminal peptides was confirmed in vitro.
    • The interaction site was mapped to the C-terminus of the p53 protein.

    Conclusions:

    • The tms1 protein directly binds to the p53 tumor suppressor.
    • This interaction involves the C-terminal domain of p53.
    • tms1 may play a role in modulating p53 function or stability.

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