Please use this identifier to cite or link to this item: https://hdl.handle.net/2440/8923
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dc.contributor.authorButt, A.-
dc.contributor.authorHarvey, N.-
dc.contributor.authorParasivam, G.-
dc.contributor.authorKumar, S.-
dc.date.issued1998-
dc.identifier.citationJournal of Biological Chemistry, 1998; 273(12):6763-6768-
dc.identifier.issn1083-351X-
dc.identifier.issn1083-351X-
dc.identifier.urihttp://hdl.handle.net/2440/8923-
dc.description.abstractNedd2 (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.-
dc.description.statementofresponsibilityAlison J. Butt, Natasha L. Harvey, Gayathri Parasivam and Sharad Kumar-
dc.language.isoen-
dc.publisherAmerican Society for Biochemistry and Molecular Biology-
dc.rights© 1998 by The American Society for Biochemistry and Molecular Biology, Inc.-
dc.subject3T3 Cells-
dc.subjectAnimals-
dc.subjectMice-
dc.subjectSaccharomyces cerevisiae-
dc.subjectEnzyme Precursors-
dc.subjectCaspases-
dc.subjectProteins-
dc.subjectRecombinant Proteins-
dc.subjectApoptosis-
dc.subjectProtein Processing, Post-Translational-
dc.subjectDimerization-
dc.subjectHydrolysis-
dc.subjectCaspase 2-
dc.titleDimerization and auto processing of the Nedd2 (caspase 2) precursor requires both the prodomain and the carboxyl-terminal regions-
dc.typeJournal article-
dc.identifier.doi10.1074/jbc.273.12.6763-
pubs.publication-statusPublished-
dc.identifier.orcidHarvey, N. [0000-0001-9839-8966]-
dc.identifier.orcidKumar, S. [0000-0001-7126-9814]-
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