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|Title:||Dimerization and auto processing of the Nedd2 (caspase 2) precursor requires both the prodomain and the carboxyl-terminal regions|
|Citation:||Journal of Biological Chemistry, 1998; 273(12):6763-6768|
|Publisher:||American Society for Biochemistry and Molecular Biology|
|Alison J. Butt, Natasha L. Harvey, Gayathri Parasivam and Sharad Kumar|
|Abstract:||Nedd2 (caspase-2) is a cysteine protease of the caspase family that has been demonstrated to play a role in the apoptotic pathway. The 51-kDa precursor of Nedd2 undergoes cleavage into two subunits following various apoptotic stimuli. In this study, we have investigated the dimerization of the Nedd2 precursor (pro-Nedd2) in Saccharomyces cerevisiae and its self-processing activity in vivo. We demonstrate that the expression of pro-Nedd2 in yeast cells results in processing of the precursor. A catalytically inactive pro-Nedd2 mutant dimerized in yeast, and the dimerization required both the prodomain and the carboxyl-terminal residues. Aspartate mutants that block the removal of the p14/p12 subunits, but not the wild-type Nedd2, were shown to dimerize in yeast cells, suggesting that dimerization occurs prior to processing. In vitro processing of pro-Nedd2 by recombinant active Nedd2 defined the aspartate residues that are crucial for processing to occur. Both the in vivo and in vitro processing of pro-Nedd2 directly correlated with its ability to induce cell death in transient overexpression experiments.|
Protein Processing, Post-Translational
|Rights:||© 1998 by The American Society for Biochemistry and Molecular Biology, Inc.|
|Appears in Collections:||Aurora harvest|
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