One-Dimensional Search Dynamics of Tumor Suppressor p53 Regulated by a Disordered C-Terminal Domain.

ABSTRACT: Tumor suppressor p53 slides along DNA and finds its target sequence in drastically different and changing cellular conditions. To elucidate how p53 maintains efficient target search at different concentrations of divalent cations such as Ca²⁺ and Mg²⁺, we prepared two mutants of p53, each possessing one of its two DNA-binding domains, the CoreTet mutant having the structured core domain plus the tetramerization (Tet) domain, and the TetCT mutant having Tet plus the disordered C-terminal domain. We investigated their equilibrium and kinetic dissociation from DNA and search dynamics along DNA at various [Mg²⁺]. Although binding of CoreTet to DNA becomes markedly weaker at higher [Mg²⁺], binding of TetCT depends slightly on [Mg²⁺]. Single

SUBMITTER: Murata A 

PROVIDER: S-EPMC5474741 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature