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Inactivating a specific protein in vivo can yield important information about its function. One strategy previously developed in Saccharomyces cerevisiae by the Varshavsky group involves fusing a degron, derived from mouse dihydrofolate reductase, to the N-terminus of the target protein, which thereby confers temperature-sensitive degradation at the restrictive temperature. We describe here the application of this technique in the fission yeast, Schizosaccharomyces pombe.

Original publication

DOI

10.1007/978-1-60327-815-7_27

Type

Journal article

Journal

Methods Mol Biol

Publication Date

2009

Volume

521

Pages

483 - 492

Keywords

Animals, Base Sequence, DNA Primers, DNA, Recombinant, Genetic Vectors, Hot Temperature, In Vitro Techniques, Mice, Molecular Sequence Data, Plasmids, Recombinant Fusion Proteins, Schizosaccharomyces, Schizosaccharomyces pombe Proteins, Tetrahydrofolate Dehydrogenase, Transformation, Genetic