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|Title:||Conversion of procaspase-3 to an autoactivating caspase by fusion to the caspase-2 predomain|
|Citation:||Journal of Biological Chemistry, 1998; 273(41):26566-26570|
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Paul A. Colussi, Natasha L. Harvey, Linda M. Shearwin-Whyatt and Sharad Kumar|
|Abstract:||Caspases are cysteine proteases that play an essential role in apoptosis. Initial activation of caspases defines the key step in apoptotic execution. Based on primary structure, caspases can be divided into two groups, those with long amino-terminal prodomains (class I), and those with relatively short prodomains (class II). On overexpression in mammalian cells, class I caspases can induce cell death that is dependent on their autocatalytic activity. Recent studies suggest that the long prodomains in some class I caspases are able to mediate dimerization of procaspase molecules, thereby promoting autoprocessing. In this communication, we demonstrate that fusion of the prodomain of a class I caspase (Nedd2/caspase-2) with procaspase-3 greatly augments autocatalysis and apoptosis induction by the chimeric caspase-3 molecule. The chimeric caspase-3 molecules were able to form homodimers in Saccharomyces cerevisiae and were efficiently processed in transfected mammalian cells. These results provide direct evidence for a role of a class I caspase prodomain in caspase autoactivation and processing and establish a basis for functional hierarchy among the two classes of caspases.|
|Keywords:||3T3 Cells; Animals; Mice; Saccharomyces cerevisiae; Enzyme Precursors; Caspases; Luminescent Proteins; Green Fluorescent Proteins; Recombinant Fusion Proteins; DNA Primers; Apoptosis; Protein Processing, Post-Translational; Enzyme Activation; Base Sequence; Dimerization; Caspase 3; Caspase 2|
|Rights:||© 1998 by The American Society for Biochemistry and Molecular Biology, Inc.|
|Appears in Collections:||Medicine publications|
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