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Nucleic Acids Research, 2001, Vol. 29, No. 10 e47
© 2001 Oxford University Press

New variants of inducible Cre recombinase: a novel mutant of Cre–PR fusion protein exhibits enhanced sensitivity and an expanded range of inducibility

Frank T. Wunderlich, Hendrik Wildner, Klaus Rajewsky and Frank Edenhofer*

Institute for Genetics, University of Cologne, Weyertal 121, D-50931 Cologne, Germany

We have developed a novel inducible Cre mutant with enhanced recombinase activity to mediate genetic switching events. The protein, designated Cre*PR, is composed of a new Cre mutant at the N-terminus followed by the ligand-binding domain (LBD) of the progesterone receptor (PR). The response to low doses of inducer is significantly enhanced by elongating the C-terminus of the PR LBD from amino acid 891 to 914. The mutant Cre lacks the first 18 amino acids and contains a Val->Ala substitution at position 336, thereby destroying a cryptic splice donor at the 3'-end of Cre. The latter mutation reduces unwanted background recombinase activity in the absence of the synthetic ligand RU486 by a factor of at least 10 to an almost undetectable level. Thus, the recombinase activity turns out to be inducible by a factor of >200. We expect Cre*PR to serve as a valuable tool for conditional expression of genes both in vitro and in vivo.

* To whom correspondence should be addressed. Tel: +49 221 470 4589; Fax: +49 221 470 5185; Email: frank.edenhofer{at}uni-koeln.de Present address: Hendrik Wildner, Max-Delbrueck-Centrum, Department of Medical Genetics, Robert-Roessle-Strasse 10, D-13125 Berlin-Buch, Germany


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