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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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

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.[1]

References

  1. Mutations in the 2-microns circle site-specific recombinase that abolish recombination without affecting substrate recognition. Prasad, P.V., Young, L.J., Jayaram, M. Proc. Natl. Acad. Sci. U.S.A. (1987) [Pubmed]
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