Mutations in the 2-microns circle site-specific recombinase that abolish recombination without affecting substrate recognition. | Zendy

Paruchuri V. Prasad | Zendy; L J Young | Zendy; Makkuni Jayaram | Zendy

Open Access

Mutations in the 2-microns circle site-specific recombinase that abolish recombination without affecting substrate recognition.

Author(s) -

Paruchuri V. Prasad,

L J Young,

Makkuni Jayaram

Publication year - 1987

Publication title -

proceedings of the national academy of sciences

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 5.011

H-Index - 771

eISSN - 1091-6490

pISSN - 0027-8424

DOI - 10.1073/pnas.84.8.2189

Subject(s) - recombinase , flp frt recombination , site specific recombination , tyrosine , cre lox recombination , mutant , dna , holliday junction , cre recombinase , recombination , biology , microbiology and biotechnology , chemistry , genetics , biochemistry , homologous recombination , genetic recombination , gene , transgene , genetically modified mouse

The site-specific recombinase encoded by the yeast plasmid 2-microns circle (FLP) forms a transient covalent linkage with its substrate DNA via a tyrosine residue, which appears to be located near its COOH terminus. The homology of the COOH terminus of FLP with that of the Int family of recombinases suggests that tyrosine-343 of FLP could be involved in forming the DNA-protein bridge. We have mutated tyrosine-343 to a phenylalanine or serine. We demonstrate that the binding of each of the two mutant proteins to its substrate is indistinguishable from that of wild-type FLP. However, both mutant proteins are incapable of catalyzing strand cleavage and recombination.

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