Nucleic Acids Research, Vol 24, Issue 8 1404-1411, Copyright © 1996 by Oxford University Press
C Kellendonk, F Tronche, AP Monaghan, PO Angrand, F Stewart and G Schutz
To create a strategy for inducible gene targeting we developed a Cre- lox
recombination system which responds to the synthetic steroid RU 486.
Several fusions between Cre recombinase and the hormone binding domain
(HBD) of a mutated human progesterone receptor, which binds RU 486 but not
progesterone, were constructed. When tested in transient expression assays
recombination activities of all fusion proteins were responsive to RU 486,
but not to the endogenous steroid progesterone. However, the observed
induction of recombination activity by the synthetic steroid varied between
the different fusion proteins. The fusion with the highest activity in the
presence of RU 486 combined with low background activity in the absence of
the steroid was tested after stable expression in fibroblast and embryonal
stem (ES) cells. We could demonstrate that its recombination activity was
highly dependent on RU 486. Since the RU 486 doses required to activate
recombination were considerably lower than doses displaying
anti-progesterone effects in mice, this system could be used as a valuable
tool for inducible gene targeting.
ARTICLES
Regulation of Cre recombinase activity by the synthetic steroid RU 486
Molecular Biology of the Cell 1, German Cancer Research Center, Heidelberg.
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