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Journal Article

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

MPS-Authors
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Fukuda,  Yoshiyuki
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Beck,  Florian
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Plitzko,  Jürgen M.
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Baumeister,  Wolfgang
Baumeister, Wolfgang / Molecular Structural Biology, Max Planck Institute of Biochemistry, Max Planck Society;

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Fulltext (public)

PNAS-2017-Fukuda-4412-7.pdf
(Publisher version), 3MB

Supplementary Material (public)

pnas.201701367SI.pdf
(Supplementary material), 3MB

Citation

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.


Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-5327-9
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.