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  • Title: GAL4 is a substrate for caspases: implications for two-hybrid screening and other GAL4-based assays.
    Author: van Criekinge W, Cornelis S, Van De Craen M, Vandenabeele P, Fiers W, Beyaert R.
    Journal: Mol Cell Biol Res Commun; 1999 May; 1(2):158-61. PubMed ID: 10356366.
    Abstract:
    Yeast two-hybrid technology as well as mammalian reporter assays use fusions between a protein of interest and the GAL4 DNA-binding domain (GAL4DB). We demonstrate that expression of a GAL4DB/caspase-1 chimeric protein in yeast leads to autoproteolytic cleavage of GAL4DB. Moreover, recombinant GAL4DB is a good in vitro substrate for recombinant caspase-1 and several other caspases. Cleavage sites map at the C-terminus of GAL4DB and result in release of the fused protein. The finding that GAL4DB can be cleaved by caspases has important implications for the use of caspases in two-hybrid analysis and in the interpretation of mammalian assays based on GAL4-dependent reporter gene expression.
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