In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes.
Identifieur interne : 000D23 ( PubMed/Curation ); précédent : 000D22; suivant : 000D24In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes.
Auteurs : Yoshiyuki Fukuda [Allemagne] ; Florian Beck [Allemagne] ; Jürgen M. Plitzko [Allemagne] ; Wolfgang Baumeister [Allemagne]Source :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2017.
Descripteurs français
- KwdFr :
- Aminopeptidases (génétique), Aminopeptidases (métabolisme), Animaux, Animaux nouveau-nés, Cellules cultivées, Conformation des protéines, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (génétique), Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (métabolisme), Liaison aux protéines, Modèles moléculaires, Neurones (métabolisme), Neurones (ultrastructure), Proteasome endopeptidase complex (), Proteasome endopeptidase complex (métabolisme), Rats, Serine endopeptidases (génétique), Serine endopeptidases (métabolisme).
- MESH :
- génétique : Aminopeptidases, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Serine endopeptidases.
- métabolisme : Aminopeptidases, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Neurones, Proteasome endopeptidase complex, Serine endopeptidases.
- Animaux, Animaux nouveau-nés, Cellules cultivées, Conformation des protéines, Liaison aux protéines, Modèles moléculaires, Neurones, Proteasome endopeptidase complex, Rats.
English descriptors
- KwdEn :
- Aminopeptidases (genetics), Aminopeptidases (metabolism), Animals, Animals, Newborn, Cells, Cultured, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (genetics), Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (metabolism), Models, Molecular, Neurons (metabolism), Neurons (ultrastructure), Proteasome Endopeptidase Complex (chemistry), Proteasome Endopeptidase Complex (metabolism), Protein Binding, Protein Conformation, Rats, Serine Endopeptidases (genetics), Serine Endopeptidases (metabolism).
- MESH :
- chemical , chemistry : Proteasome Endopeptidase Complex.
- chemical , genetics : Aminopeptidases, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Serine Endopeptidases.
- chemical , metabolism : Aminopeptidases, Dipeptidyl-Peptidases and Tripeptidyl-Peptidases, Proteasome Endopeptidase Complex, Serine Endopeptidases.
- metabolism : Neurons.
- ultrastructure : Neurons.
- Animals, Animals, Newborn, Cells, Cultured, Models, Molecular, Protein Binding, Protein Conformation, Rats.
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 ∼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.
DOI: 10.1073/pnas.1701367114
PubMed: 28396430
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pubmed:28396430Le document en format XML
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<front><div type="abstract" xml:lang="en">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.</div>
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<Abstract><AbstractText>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.</AbstractText>
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