Binding of Rad51 and other peptide sequences to a promiscuous, highly electrostatic binding site in p53

Assaf Friedler, Dmitry B. Veprintsev, Trevor Rutherford, Karoly I. Von Glos, Alan R. Fersht*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

55 Scopus citations

Abstract

Homologous recombination is repressed by the binding of p53 to Rad51. We identified by fluorescence and NMR spectroscopy that peptides corresponding to residues 179-190 of Rad51 bind to the core domain of p53 in a site that overlaps with its specific DNA binding site. The p53 site is quite promiscuous, since it also binds peptides derived from 53BP1, 53BP2, Hif-1α, and BCL-X L in overlapping regions. Binding is mediated mainly by a strong, nonspecific, electrostatic component and is fine tuned by specific interactions. Competition of the different proteins with each other and with specific DNA for a single site in p53 could be a factor in regulation of its activity.

Original languageAmerican English
Pages (from-to)8051-8059
Number of pages9
JournalJournal of Biological Chemistry
Volume280
Issue number9
DOIs
StatePublished - 4 Mar 2005

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