Crossref journal-article
American Association for the Advancement of Science (AAAS)
Science (221)
Abstract

The catalytic mechanism of the 20 S proteasome from the archaebacterium Thermoplasma acidophilum has been analyzed by site-directed mutagenesis of the β 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 β subunits. The conservation pattern of this residue in eukaryotic sequences suggests that at least three of the seven eukaryotic β-type subunit branches should be proteolytically inactive.

Bibliography

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.

Authors 6
  1. Erika Seemüller (first)
  2. Andrei Lupas (additional)
  3. Daniela Stock (additional)
  4. Jan Löwe (additional)
  5. Robert Huber (additional)
  6. Wolfgang Baumeister (additional)
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Dates
Type When
Created 18 years, 10 months ago (Oct. 27, 2006, 2:19 p.m.)
Deposited 1 year, 7 months ago (Jan. 14, 2024, 11:45 p.m.)
Indexed 3 months, 1 week ago (May 22, 2025, 5:48 a.m.)
Issued 30 years, 4 months ago (April 28, 1995)
Published 30 years, 4 months ago (April 28, 1995)
Published Print 30 years, 4 months ago (April 28, 1995)
Funders 0

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@article{Seem_ller_1995, title={Proteasome from Thermoplasma acidophilum  : a Threonine Protease}, volume={268}, ISSN={1095-9203}, url={http://dx.doi.org/10.1126/science.7725107}, DOI={10.1126/science.7725107}, number={5210}, journal={Science}, publisher={American Association for the Advancement of Science (AAAS)}, author={Seemüller, Erika and Lupas, Andrei and Stock, Daniela and Löwe, Jan and Huber, Robert and Baumeister, Wolfgang}, year={1995}, month=apr, pages={579–582} }