Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains
Regulation of Cre recombinase activity by mutated estrogen receptor ligand-binding domains
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DOI:
10.1006/bbrc.1997.7124
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发表时间:
1997-08-28
影响因子:
3.1
通讯作者:
Chambon, P
中科院分区:
文献类型:
--
作者:
Feil, R;Wagner, J;Chambon, P
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 (LED). Two new ligand-dependent recombinases which contain either the G400V/M543A/L544A or the G400V/L539A/L540A triple mutation of the human ER LED are efficiently induced by the synthetic ER antagonists 4-hydroxytamoxifen (OHT) and ICI 182,780 (ICI), respectively, but are insensitive to 17 beta-oestradiol (E2). Both chimeric recombinases should be useful for efficient spatio-temporally controlled site-directed somatic mutagenesis. (C) 1997 Academic Press.