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.

Bibliographic Details
Main Authors: Eva M. Huber, Wolfgang Heinemeyer, Xia Li, Cassandra S. Arendt, Mark Hochstrasser, Michael Groll
Format: Article
Language:English
Published: Nature Publishing Group 2016-03-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms10900
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spelling 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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