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  Proteasome from thermoplasma acidophilum - a threonine protease

Seemüller, E., Lupas, A., Stock, D., Löwe, J., Huber, R., & Baumeister, W. (1995). Proteasome from thermoplasma acidophilum - a threonine protease. Science, 268(5210), 579-582.

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Seemüller, E.1, Author              
Lupas, A.1, Author              
Stock, D., Author
Löwe, J., Author
Huber, R.1, Author              
Baumeister, W.1, Author              
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1External Organizations, ou_persistent22              

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Free keywords: Multicatalytic proteinase complex; Electron-microscopy; Escherichia-coli; Expression; Subunits; Proteolysis; Pituitary; Sequence; Distinct; Interferon.; Multidisciplinary. Multidisciplinary. Multidisciplinary.
 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. [References: 60]

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 Dates: 1995-04-28
 Publication Status: Published in print
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 Identifiers: eDoc: 318445
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Title: Science
Source Genre: Journal
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Pages: - Volume / Issue: 268 (5210) Sequence Number: - Start / End Page: 579 - 582 Identifier: -