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Nucleic Acids Research, 2003, Vol. 31, No. 12 3050-3056
© 2003 Oxford University Press

Single-chain Tet transregulators

Christel Krueger, Christian Berens, Andreas Schmidt, Dirk Schnappinger and Wolfgang Hillen

Lehrstuhl für Mikrobiologie, Friedrich-Alexander Universität Erlangen-Nürnberg, Staudtstraße 5, D-91058 Erlangen, Germany

*To whom correspondence should be addressed. Tel: +49 9131 852 8081; Fax: +49 9131 852 8082; Email: whillen{at}biologie.uni-erlangen.de
Present address:
Dirk Schnappinger, Department of Microbiology and Immunology, Weill Medical College of Cornell University, 1300 York Avenue, Box 62, New York, NY 10021, USA

We demonstrate here that the Tet repressor (TetR), a dimeric allosterical regulatory protein, can be converted to a fully functional monomer when connected by a 29 amino acid linker. TetR-based transregulators are widely used to regulate gene expression in eukaryotes. They can be fused to form single-chain (sc) Tet transregulators with two TetR moieties and one eukaryotic regulatory domain. Sc variants of transactivator and transsilencer exhibit the same regulatory properties as their respective dimeric counterparts in human cell lines. In particular, the reverse ‘tet-on’ phenotype of rtTA variants is also present in the sc variants. Coexpression of a reverse transactivator and sc transsilencer leads to reduced background expression and shows full activation upon induction. The data demonstrate that sc Tet transregulators exhibit the phenotype of their respective dimers and lack functional interference when coexpressed in the same cell.


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