Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains
R Feil, J Wagner, D Metzger, P Chambon - Biochemical and biophysical …, 1997 - Elsevier
R Feil, J Wagner, D Metzger, P Chambon
Biochemical and biophysical research communications, 1997•ElsevierLigand-dependent chimeric Cre recombinases are powerful tools to induce specific DNA
rearrangements in cultured cells and in mice. We report here the construction and
characterization of a series of chimeric recombinases, each consisting of Cre fused to a
mutated human oestrogen receptor (ER) ligand-binding domain (LBD). Two new ligand-
dependent recombinases which contain either the G400V/M543A/L544A or the
G400V/L539A/L540A triple mutation of the human ER LBD are efficiently induced by the …
rearrangements in cultured cells and in mice. We report here the construction and
characterization of a series of chimeric recombinases, each consisting of Cre fused to a
mutated human oestrogen receptor (ER) ligand-binding domain (LBD). Two new ligand-
dependent recombinases which contain either the G400V/M543A/L544A or the
G400V/L539A/L540A triple mutation of the human ER LBD are efficiently induced by the …
Ligand-dependent chimeric Cre recombinases are powerful tools to induce specific DNA rearrangements in cultured cells and in mice. We report here the construction and characterization of a series of chimeric recombinases, each consisting of Cre fused to a mutated human oestrogen receptor (ER) ligand-binding domain (LBD). Two new ligand-dependent recombinases which contain either the G400V/M543A/L544A or the G400V/L539A/L540A triple mutation of the human ER LBD are efficiently induced by the synthetic ER antagonists 4-hydroxytamoxifen (OHT) and ICI 182,780 (ICI), respectively, but are insensitive to 17β-oestradiol (E2). Both chimeric recombinases should be useful for efficient spatio-temporally controlled site-directed somatic mutagenesis.
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