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  Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating

Eisele, M. R., Reed, R. G., Rudack, T., Schweitzer, A., Beck, F., Nagy, I., et al. (2018). Expanded Coverage of the 26S Proteasome Conformational Landscape Reveals Mechanisms of Peptidase Gating. Cell Reports, 24(5), 1301-1315.e5. doi:10.1016/j.celrep.2018.07.004.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0001-F918-C Version Permalink: http://hdl.handle.net/21.11116/0000-0001-F919-B
Genre: Journal Article

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 Creators:
Eisele, Markus R.1, Author              
Reed, Randi G.2, Author
Rudack, Till2, Author
Schweitzer, Andreas1, Author              
Beck, Florian1, Author              
Nagy, Istvan1, Author              
Pfeifer, Günter1, Author              
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Tomko Jr., Robert J.2, Author
Sakata, Eri1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              
2external, ou_persistent22              

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Free keywords: CRYO-EM STRUCTURE; REGULATORY PARTICLE; MOLECULAR-DYNAMICS; 20S PROTEASOMES; CORE PARTICLE; C-TERMINI; CRYOELECTRON MICROSCOPY; SUBSTRATE DEGRADATION; EUKARYOTIC PROTEASOME; STRUCTURAL BASISCell Biology;
 Abstract: The proteasome is the central protease for intracellular protein breakdown. Coordinated binding and hydrolysis of ATP by the six proteasomal ATPase subunits induces conformational changes that drive the unfolding and translocation of substrates into the proteolytic 20S core particle for degradation. Here, we combine genetic and biochemical approaches with cryo-electron microscopy and integrative modeling to dissect the relationship between individual nucleotide binding events and proteasome conformational dynamics. We demonstrate unique impacts of ATP binding by individual ATPases on the proteasome conformational distribution and report two conformational states of the proteasome suggestive of a rotary ATP hydrolysis mechanism. These structures, coupled with functional analyses, reveal key roles for the ATPases Rpt1 and Rpt6 in gating substrate entry into the core particle. This deepened knowledge of proteasome conformational dynamics reveals key elements of intersubunit communication within the proteasome and clarifies the regulation of substrate entry into the proteolytic chamber.

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Language(s): eng - English
 Dates: 2018
 Publication Status: Published in print
 Pages: 20
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 Table of Contents: -
 Rev. Method: -
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Project name : Excellence Cluster CIPSM to W.B.
Grant ID : -
Funding program : Excellence Cluster CIPSM
Funding organization : German Science Foundation
Project name : SFB-1035/Project A01 to W.B. and E.S.
Grant ID : -
Funding program : SFB-1035/Project A01
Funding organization : German Science Foundation

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Title: Cell Reports
Source Genre: Journal
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Publ. Info: Maryland Heights, MO : Cell Press
Pages: - Volume / Issue: 24 (5) Sequence Number: - Start / End Page: 1301 - 1315.e5 Identifier: ISSN: 2211-1247
CoNE: https://pure.mpg.de/cone/journals/resource/2211-1247