Ontology highlight
ABSTRACT:
SUBMITTER: Olorunniji FJ
PROVIDER: S-EPMC2794168 | biostudies-literature | 2009 Dec
REPOSITORIES: biostudies-literature
Olorunniji Femi J FJ Stark W Marshall WM
Nucleic acids research 20091201 22
To characterize the residues that participate in the catalysis of DNA cleavage and rejoining by the site-specific recombinase Tn3 resolvase, we mutated conserved polar or charged residues in the catalytic domain of an activated resolvase variant. We analysed the effects of mutations at 14 residues on proficiency in binding to the recombination site ('site I'), formation of a synaptic complex between two site Is, DNA cleavage and recombination. Mutations of Y6, R8, S10, D36, R68 and R71 resulted ...[more]