A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome

Eva M. Huber; Wolfgang Heinemeyer; Xia Li; Cassandra S. Arendt; Mark Hochstrasser; Michael Groll

doi:10.1038/ncomms10900

Nature Communications (Mar 2016)

A unified mechanism for proteolysis and autocatalytic activation in the 20S proteasome

Eva M. Huber,
Wolfgang Heinemeyer,
Xia Li,
Cassandra S. Arendt,
Mark Hochstrasser,
Michael Groll

Affiliations

Eva M. Huber: Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität München
Wolfgang Heinemeyer: Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität München
Xia Li: Department of Molecular Biophysics and Biochemistry, Yale University
Cassandra S. Arendt: Department of Biochemistry and Molecular Biology, University of Chicago
Mark Hochstrasser: Department of Molecular Biophysics and Biochemistry, Yale University
Michael Groll: Center for Integrated Protein Science at the Department Chemie, Lehrstuhl für Biochemie, Technische Universität München

DOI: https://doi.org/10.1038/ncomms10900
Journal volume & issue: Vol. 7, no. 1
pp. 1 – 10

Abstract

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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.

Published in Nature Communications

ISSN: 2041-1723 (Online)
Publisher: Nature Portfolio
Country of publisher: United Kingdom
LCC subjects: Science
Website: https://www.nature.com/ncomms/

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