In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes.
Identifieur interne : 000C60 ( PubMed/Checkpoint ); précédent : 000C59; suivant : 000C61In 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
Affiliations:
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Endopeptidase Complex (chemistry)</term><term>Proteasome Endopeptidase Complex (metabolism)</term><term>Protein Binding</term><term>Protein Conformation</term><term>Rats</term><term>Serine Endopeptidases (genetics)</term><term>Serine Endopeptidases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Aminopeptidases (génétique)</term><term>Aminopeptidases (métabolisme)</term><term>Animaux</term><term>Animaux nouveau-nés</term><term>Cellules cultivées</term><term>Conformation des protéines</term><term>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (génétique)</term><term>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases (métabolisme)</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Neurones (métabolisme)</term><term>Neurones (ultrastructure)</term><term>Proteasome endopeptidase complex ()</term><term>Proteasome endopeptidase complex (métabolisme)</term><term>Rats</term><term>Serine endopeptidases (génétique)</term><term>Serine endopeptidases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Proteasome Endopeptidase Complex</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Aminopeptidases</term><term>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Aminopeptidases</term><term>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</term><term>Proteasome Endopeptidase Complex</term><term>Serine Endopeptidases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Aminopeptidases</term><term>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Neurons</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Aminopeptidases</term><term>Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</term><term>Neurones</term><term>Proteasome endopeptidase complex</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Neurons</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Animals, Newborn</term><term>Cells, Cultured</term><term>Models, Molecular</term><term>Protein Binding</term><term>Protein Conformation</term><term>Rats</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Animaux nouveau-nés</term><term>Cellules cultivées</term><term>Conformation des protéines</term><term>Liaison aux protéines</term><term>Modèles moléculaires</term><term>Neurones</term><term>Proteasome endopeptidase complex</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><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></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28396430</PMID><DateCompleted><Year>2018</Year><Month>05</Month><Day>15</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>114</Volume><Issue>17</Issue><PubDate><Year>2017</Year><Month>04</Month><Day>25</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>In situ structural studies of tripeptidyl peptidase II (TPPII) reveal spatial association with proteasomes.</ArticleTitle><Pagination><MedlinePgn>4412-4417</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.1701367114</ELocationID><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></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fukuda</LastName><ForeName>Yoshiyuki</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Beck</LastName><ForeName>Florian</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Plitzko</LastName><ForeName>Jürgen M</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Baumeister</LastName><ForeName>Wolfgang</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, 82152 Martinsried, Germany baumeist@biochem.mpg.de.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>04</Month><Day>10</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>EC 3.4.11.-</RegistryNumber><NameOfSubstance UI="D000626">Aminopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.14.-</RegistryNumber><NameOfSubstance UI="D004152">Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.14.10</RegistryNumber><NameOfSubstance UI="C048001">tripeptidyl-peptidase 2</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.-</RegistryNumber><NameOfSubstance UI="D012697">Serine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.25.1</RegistryNumber><NameOfSubstance UI="D046988">Proteasome Endopeptidase Complex</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.99.-</RegistryNumber><NameOfSubstance UI="C061553">ATP dependent 26S protease</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000626" MajorTopicYN="N">Aminopeptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000831" MajorTopicYN="N">Animals, Newborn</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004152" MajorTopicYN="N">Dipeptidyl-Peptidases and Tripeptidyl-Peptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009474" MajorTopicYN="N">Neurons</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046988" MajorTopicYN="N">Proteasome Endopeptidase Complex</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D012697" MajorTopicYN="N">Serine Endopeptidases</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">26S proteasome</Keyword><Keyword MajorTopicYN="Y">Volta phase plate</Keyword><Keyword MajorTopicYN="Y">cryo-electron tomography</Keyword><Keyword MajorTopicYN="Y">primary cultured neuronal cell</Keyword><Keyword MajorTopicYN="Y">subtomogram averaging</Keyword></KeywordList><CoiStatement>The authors declare no conflict of interest.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>4</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>5</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2017</Year><Month>4</Month><Day>12</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">28396430</ArticleId><ArticleId IdType="pii">1701367114</ArticleId><ArticleId IdType="doi">10.1073/pnas.1701367114</ArticleId><ArticleId 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sortKey="Baumeister, Wolfgang" sort="Baumeister, Wolfgang" uniqKey="Baumeister W" first="Wolfgang" last="Baumeister">Wolfgang Baumeister</name><name sortKey="Beck, Florian" sort="Beck, Florian" uniqKey="Beck F" first="Florian" last="Beck">Florian Beck</name><name sortKey="Plitzko, Jurgen M" sort="Plitzko, Jurgen M" uniqKey="Plitzko J" first="Jürgen M" last="Plitzko">Jürgen M. 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