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Yeast As a Chassis for Developing Functional Assays to Study Human P53
Published on: August 4, 2019
Structural Evolution and Dynamics of the p53 Proteins
Giovanni Chillemi1, Sebastian Kehrloesser2, Francesca Bernassola3
1CINECA, SCAI-SuperComputing Applications and Innovation Department, Rome 00185, Italy.
Abstract:
The family of the p53 tumor suppressive transcription factors includes p73 and p63 in addition to p53 itself. Given the high degree of amino-acid-sequence homology and structural organization shared by the p53 family members, they display some common features (i.e., induction of cell death, cell-cycle arrest, senescence, and metabolic regulation in response to cellular stress) as well as several distinct properties. Here, we describe the structural evolution of the family members with recent advances on the molecular dynamic studies of p53 itself. A crucial role of the carboxy-terminal domain in regulating the properties of the DNA-binding domain (DBD) supports an induced-fit mechanism, in which the binding of p53 on individual promoters is preferentially regulated by the KOFF over KON.
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