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  Localization of the regulatory particle subunit Semi in the 26S proteasome

Bohn, S., Sakata, E., Beck, F., Pathare, G. R., Schnitger, J., Nagy, I., et al. (2013). Localization of the regulatory particle subunit Semi in the 26S proteasome. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 435(2), 250-254. doi:10.1016/j.bbrc.2013.04.069.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-4553-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0014-4554-7
Genre: Journal Article

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 Creators:
Bohn, Stefan1, Author              
Sakata, Eri1, Author              
Beck, Florian1, Author              
Pathare, Ganesh Ramnath1, Author              
Schnitger, Jérôme1, Author              
Nagy, Istvan1, Author              
Baumeister, Wolfgang1, Author              
Förster, Friedrich1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: CHEMICAL CROSS-LINKING; MESSENGER-RNA EXPORT; SACCHAROMYCES-CEREVISIAE; 20S PROTEASOME; YEAST; PROTEIN; RESOLUTION; ARCHITECTURE; MICROSCOPY; COMPONENT26S proteasome; Sem1; Proteasome-COP9-initiation factor domain; TREX-2; Cryo-electron microscopy;
 Abstract: The ubiquitin-proteasome system is responsible for regulated protein degradation in the cell with the 26S proteasome acting as its executive arm. The molecular architecture of this 2.5 MDa complex has been established recently, with the notable exception of the small acidic subunit Semi. Here, we localize the C-terminal helix of Semi binding to the PCI domain of the subunit Rpn7 using cryo-electron microscopy single particle reconstruction of proteasomes purified from yeast cells with semi deletion. The approximate position of the N-terminal region of Semi bridging the cleft between Rpn7 and Rpn3 was inferred based on site-specific cross-linking data of the 26S proteasome. Our structural studies indicate that Semi can assume different conformations in different contexts, which supports the idea that Semi functions as a molecular glue stabilizing the Rpn3/Rpn7 heterodimer. (C) 2013 Elsevier Inc. All rights reserved.

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Language(s): eng - English
 Dates: 2013
 Publication Status: Published in print
 Pages: 5
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Degree: -

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Title: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Source Genre: Journal
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Publ. Info: 525 B ST, STE 1900, SAN DIEGO, CA 92101-4495 USA : ACADEMIC PRESS INC ELSEVIER SCIENCE
Pages: - Volume / Issue: 435 (2) Sequence Number: - Start / End Page: 250 - 254 Identifier: ISSN: 0006-291X