A rationally designed peptide enhances homologous recombination in vitro and resistance to DNA damaging agents in vivo.

ABSTRACT: The RecA family of proteins is essential in homologous recombination, a critical step in DNA repair. Here, we report that a rationally-designed small peptide based on the crystal structure of Escherichia coli RecA-DNA complex can promote homologous recombination through the enhancement of both RecA-mediated strand assimilation and three-strand exchange activity. Among 17 peptides tested, peptide #3 with the amino acid sequence of IRFLTARRR has the most potent activity in promoting the RecA-mediated D-loop formation by approximately 7.2-fold at 37 degrees C. Other peptides such as IRFLTAKKK and IRLLTARRR also have similar, albeit lower, activities. Therefore, hydrophobicity and poly-positive charges, and the space between them in those small peptides are crucial features for such activities

SUBMITTER: Chen LT 

PROVIDER: S-EPMC2910059 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature