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https://hdl.handle.net/2440/8923
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Type: | Journal article |
Title: | Dimerization and auto processing of the Nedd2 (caspase 2) precursor requires both the prodomain and the carboxyl-terminal regions |
Author: | Butt, A. Harvey, N. Parasivam, G. Kumar, S. |
Citation: | Journal of Biological Chemistry, 1998; 273(12):6763-6768 |
Publisher: | American Society for Biochemistry and Molecular Biology |
Issue Date: | 1998 |
ISSN: | 1083-351X 1083-351X |
Statement of Responsibility: | 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. |
Keywords: | 3T3 Cells Animals Mice Saccharomyces cerevisiae Enzyme Precursors Caspases Proteins Recombinant Proteins Apoptosis Protein Processing, Post-Translational Dimerization Hydrolysis Caspase 2 |
Rights: | © 1998 by The American Society for Biochemistry and Molecular Biology, Inc. |
DOI: | 10.1074/jbc.273.12.6763 |
Published version: | http://dx.doi.org/10.1074/jbc.273.12.6763 |
Appears in Collections: | Aurora harvest Medicine publications |
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