Protein expression can be monitored in yeast by peptide-mediated induction of TetR-controlled gene expression.

Christoph Stoeckle, Marcus Klotzsche, Wolfgang Hillen

Lehrstuhl für Mikrobiologie, Department Biologie, Friedrich-Alexander-Universität Erlangen-Nürnberg, Staudtstrasse 5, 91058 Erlangen, Germany.

Journal of biotechnology 2012 Oct 31

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The rapidly increasing number of completed genome sequences urgently calls for convenient and efficient methods for analysis of gene function and expression. TetR-inducing peptides (TIP) can induce reporter gene expression controlled by Tet repressor (TetR) when fused to a protein of choice which makes them a highly valuable tool for monitoring expression in vivo. However, TIP functionality has only been demonstrated in bacteria so far. Here, we report that TIP is also functional in yeast. An mCherry-TIP fusion that locates to the nucleus induces TetR-controlled gfp+ expression in a dose-dependent manner. This opens up potential applications in proteome research in which the expression of proteins can be analyzed in vivo by fusing TIP to proteins of choice in conjunction with a Tet-controlled reporter system. Copyright © 2012 Elsevier B.V. All rights reserved.

Citation

Christoph Stoeckle, Marcus Klotzsche, Wolfgang Hillen. Protein expression can be monitored in yeast by peptide-mediated induction of TetR-controlled gene expression. Journal of biotechnology. 2012 Oct 31;161(3):265-8