Two structural features of lambda integrase that are critical for DNA cleavage by multimers but not by monomers.

ABSTRACT: Despite many years of genetic and biochemical studies on the lambda integrase (Int) recombination system, it is still not known whether the Int protein is competent for DNA cleavage as a monomer. We have addressed this question, as part of a larger study of Int functions critical for the formation of higher-order complexes, by isolating "multimer-specific" mutants. We identify a pair of oppositely charged residues, E153 and R169, that comprise an intermolecular salt bridge within a functional Int multimer. Mutation of either of these residues significantly reduces both the cleavage of full-att sites and the resolution of Holliday junctions without compromising the cleavage of half-att site substrates. Allele-specific suppressor mutations were generated at these residues. Their interaction

SUBMITTER: Lee SY 

PROVIDER: S-EPMC365695 | biostudies-literature | 2004 Mar

REPOSITORIES: biostudies-literature