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| Title | In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes. |
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| Journal, issue, pages | Proc Natl Acad Sci U S A, Vol. 114, Issue 17, Page 4412-4417, Year 2017 |
| Publish date | Apr 25, 2017 |
 Authors | Yoshiyuki Fukuda / Florian Beck / Jürgen M Plitzko / Wolfgang Baumeister /  |
| PubMed 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 ...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 ∼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. |
 External links | Proc Natl Acad Sci U S A / PubMed:28396430 / PubMed Central |
| Methods | EM (subtomogram averaging) |
| Resolution | 27.8 - 36.5 Å |
| Structure data |  EMDB-4119:  EMDB-4120: |
| Source |
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Rattus (rat)
