Proteolytic mechanism of a novel mitochondrial and chloroplastic PreP peptidasome
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Shashi Bhushan
, Kenneth A. Johnson , Therese Eneqvist and Elzbieta Glaser
Abstract
The 2.1-Å-resolution crystal structure of the novel mitochondrial and chloroplastic metalloendopeptidase, AtPreP1, revealed a unique peptidasome structure, in which the two halves of the enzyme completely enfold a huge proteolytic cavity. Based on the structure, we proposed a novel mechanism for proteolysis involving hinge-bending motions, which cause the protease to open and close in response to substrate binding. We generated four double-mutants of AtPreP1 by introducing cysteines at positions where disulfide bonds can be formed in order to lock and unlock the protease and tested the activity under oxidizing and reducing conditions. The overall results support the proposed mechanism.
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©2006 by Walter de Gruyter Berlin New York
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Articles in the same Issue
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- Regulation of human cathepsin B by alternative mRNA splicing: homeostasis, fatal errors and cell death
- The peptidases from fungi and viruses
- C. elegans as a model system to study the function of the COG complex in animal development
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- Single-cell resolution imaging of membrane-anchored hepatitis C virus NS3/4A protease activity
- Treatment of MCF-7 cells with taxol and etoposide induces distinct alterations in the expression of apoptosis-related genes BCL2, BCL2L12, BAX, CASPASE-9 and FAS
- Proteolytic mechanism of a novel mitochondrial and chloroplastic PreP peptidasome
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- Molecular and functional analysis of new members of the wheat PR4 gene family
- C-Terminal truncations of syncytin-1 (ERVWE1 envelope) that increase its fusogenicity
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