A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome
The proteasome, an essential molecular machine, is a threonine protease, but the evolution and the components of its proteolytic centre are unclear. Here, the authors use structural biology and biochemistry to investigate the role of proteasome active site residues on maturation and activity.
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2016-03-01
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Series: | Nature Communications |
Online Access: | https://doi.org/10.1038/ncomms10900 |
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doaj-8d736013f95044c8b26f6406a2319c6e2021-05-11T11:13:47ZengNature Publishing GroupNature Communications2041-17232016-03-017111010.1038/ncomms10900A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasomeEva M. Huber0Wolfgang Heinemeyer1Xia Li2Cassandra S. Arendt3Mark Hochstrasser4Michael Groll5Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität MünchenCenter for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität MünchenDepartment of Molecular Biophysics and Biochemistry, Yale UniversityDepartment of Biochemistry and Molecular Biology, University of ChicagoDepartment of Molecular Biophysics and Biochemistry, Yale UniversityCenter for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität MünchenThe proteasome, an essential molecular machine, is a threonine protease, but the evolution and the components of its proteolytic centre are unclear. Here, the authors use structural biology and biochemistry to investigate the role of proteasome active site residues on maturation and activity.https://doi.org/10.1038/ncomms10900 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Eva M. Huber Wolfgang Heinemeyer Xia Li Cassandra S. Arendt Mark Hochstrasser Michael Groll |
spellingShingle |
Eva M. Huber Wolfgang Heinemeyer Xia Li Cassandra S. Arendt Mark Hochstrasser Michael Groll A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome Nature Communications |
author_facet |
Eva M. Huber Wolfgang Heinemeyer Xia Li Cassandra S. Arendt Mark Hochstrasser Michael Groll |
author_sort |
Eva M. Huber |
title |
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome |
title_short |
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome |
title_full |
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome |
title_fullStr |
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome |
title_full_unstemmed |
A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome |
title_sort |
unified mechanism for proteolysis and autocatalytic activation in the 20s proteasome |
publisher |
Nature Publishing Group |
series |
Nature Communications |
issn |
2041-1723 |
publishDate |
2016-03-01 |
description |
The proteasome, an essential molecular machine, is a threonine protease, but the evolution and the components of its proteolytic centre are unclear. Here, the authors use structural biology and biochemistry to investigate the role of proteasome active site residues on maturation and activity. |
url |
https://doi.org/10.1038/ncomms10900 |
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