Article
The Disordered Linker in p53 Participates in Nonspecific Binding to and One-Dimensional Sliding along DNA Revealed by Single-Molecule Fluorescence Measurements.
Biochemistry - 15 Aug 2017
Subekti Dwiky Rendra Graha, Murata Agato, Itoh Yuji, Fukuchi Satoshi, Takahashi Hiroto, Kanbayashi Saori, Takahashi Satoshi, Kamagata Kiyoto
Abstract excerpt
The tumor suppressor p53 is a multidomain transcription factor that can quickly bind to its target DNA by sliding along the DNA strand. We hypothesized that the intrinsically disordered and positively charged linker of p53 regulates its search dynamics first by directly interacting with DNA and second by modulating hopping of the core domain. To test the two hypotheses, we prepared five variants of p53 in which...
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