Journal article
Cleavage-dependent Ligation by the FLP Recombinase CHARACTERIZATION OF A MUTANT FLP PROTEIN WITH AN ALTERATION IN A CATALYTIC AMINO ACID (∗)
Abstract
The FLP recombinase of the 2 microM plasmid of Saccharomyces cerevisiae belongs to the integrase family of recombinases whose members have in common four absolutely conserved residues (Arg-191, His-305, Arg-308, and Tyr-343). We have studied the mutant protein FLP R308K in which the arginine residue at position 308 has been replaced by lysine. Although FLP R308K was previously reported to be defective in ligation of certain substrates (Pan, G., …
Authors
Zhu X-D; Sadowski PD
Journal
Journal of Biological Chemistry, Vol. 270, No. 39, pp. 23044–23054
Publisher
Elsevier
Publication Date
September 1995
DOI
10.1074/jbc.270.39.23044
ISSN
0021-9258
Associated Experts
Fields of Research (FoR)
Medical Subject Headings (MeSH)
Amino Acid SequenceBase SequenceBinding SitesConserved SequenceDNA NucleotidyltransferasesFungal ProteinsLigasesModels, GeneticModels, StructuralMolecular Sequence DataMutagenesis, Site-DirectedOligodeoxyribonucleotidesPlasmidsPoint MutationRecombinant ProteinsRecombination, GeneticSaccharomyces cerevisiaeSubstrate Specificity