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  In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes

Fukuda, Y., Beck, F., Plitzko, J. M., & Baumeister, W. (2017). In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes. Proceedings of the National Academy of Sciences of the United States of America, 114(17), 4412-4417. doi:10.1073/pnas.1701367114.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-5327-9 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-5328-7
Genre: Journal Article

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 Creators:
Fukuda, Yoshiyuki1, Author              
Beck, Florian1, Author              
Plitzko, Jürgen M.1, Author              
Baumeister, Wolfgang1, Author              
Affiliations:
1Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565142              

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Free keywords: CRYOELECTRON TOMOGRAPHY; ANTIGEN PRESENTATION; GIANT PROTEASE; PHASE PLATE; DEGRADATION; CLASSIFICATION; VISUALIZATION; SUBTOMOGRAMS; DROSOPHILA; TOOLBOXScience & Technology - Other Topics; primary cultured neuronal cell; 26S proteasome; Volta phase plate; cryo-electron tomography; subtomogram averaging;
 Abstract: Tripeptidyl peptidase II (TPPII) is a eukaryotic protease acting downstream of the 26S proteasome; it removes tripeptides from the degradation products released by the proteasome. Structural studies in vitro have revealed the basic architecture of TPPII, a two-stranded linear polymer that assembles to form a spindle-shaped complex of similar to 6 MDa. Dependent on protein concentration, TPPII has a distinct tendency for polymorphism. Therefore, its structure in vivo has remained unclear. To resolve this issue, we have scrutinized cryo-electron tomograms of rat hippocampal neurons for the occurrence and spatial distribution of TPPII by template matching. The quality of the tomograms recorded with the Volta phase plate enabled a detailed structural analysis of TPPII despite its low abundance. Two different assembly states (36-mers and 32-mers) coexist as well as occasional extended forms with longer strands. A distance analysis of the relative locations of TPPII and 26S proteasomes confirmed the visual impression that these two complexes spatially associate in agreement with TPPII's role in postproteasomal degradation.

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Language(s): eng - English
 Dates: 2017-04-102017
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Method: -
 Identifiers: ISI: 000399995600053
DOI: 10.1073/pnas.1701367114
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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : Proc. Acad. Sci. USA
  Other : Proc. Acad. Sci. U.S.A.
  Abbreviation : PNAS
Source Genre: Journal
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Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 114 (17) Sequence Number: - Start / End Page: 4412 - 4417 Identifier: ISSN: 0027-8424
CoNE: /journals/resource/954925427230