TY - JOUR
T1 - Binding of Rad51 and other peptide sequences to a promiscuous, highly electrostatic binding site in p53
AU - Friedler, Assaf
AU - Veprintsev, Dmitry B.
AU - Rutherford, Trevor
AU - Von Glos, Karoly I.
AU - Fersht, Alan R.
PY - 2005/3/4
Y1 - 2005/3/4
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=14844314815&partnerID=8YFLogxK
U2 - 10.1074/jbc.M411176200
DO - 10.1074/jbc.M411176200
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C2 - 15611070
AN - SCOPUS:14844314815
SN - 0021-9258
VL - 280
SP - 8051
EP - 8059
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 9
ER -
