Proteasome from Thermoplasma acidophilum: a threonine protease
- PMID: 7725107
- DOI: 10.1126/science.7725107
Proteasome from Thermoplasma acidophilum: a threonine protease
Abstract
The catalytic mechanism of the 20S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the beta subunit and by inhibitor studies. Deletion of the amino-terminal threonine or its mutation to alanine led to inactivation of the enzyme. Mutation of the residue to serine led to a fully active enzyme, which was over ten times more sensitive to the serine protease inhibitor 3,4-dichloroisocoumarin. In combination with the crystal structure of a proteasome-inhibitor complex, the data show that the nucleophilic attack is mediated by the amino-terminal threonine of processed beta subunits. The conservation pattern of this residue in eukaryotic sequences suggests that at least three of the seven eukaryotic beta-type subunit branches should be proteolytically inactive.
Comment in
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From the cradle to the grave: ring complexes in the life of a protein.Science. 1995 Apr 28;268(5210):523-4. doi: 10.1126/science.7725096. Science. 1995. PMID: 7725096 Review. No abstract available.
Comment on
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Functions of the proteasome: the lysis at the end of the tunnel.Science. 1995 Apr 28;268(5210):522-3. doi: 10.1126/science.7725095. Science. 1995. PMID: 7725095 Review. No abstract available.
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