Assembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexes.

ATPases Associated with Diverse Cellular Activities / chemistry Apoptosis Regulatory Proteins / chemistry Binding Sites Carrier Proteins / chemistry Chromatography, Gel DNA Helicases / chemistry Humans Models, Molecular Multiprotein Complexes / chemistry Protein Conformation Protein Domains Protein Structure, Quaternary
AAA+ proteins ATPases PAQosome R2TP RUVBL1/2 macromolecular complex assembly molecular chaperones protein folding

Journal

Structure (London, England : 1993)
ISSN: 1878-4186
Titre abrégé: Structure
Pays: United States
ID NLM: 101087697

Informations de publication

Date de publication:
06 01 2022
Historique:
received: 19 04 2021
revised: 16 07 2021
accepted: 10 08 2021
pubmed: 8 9 2021
medline: 22 3 2022
entrez: 7 9 2021
Statut: ppublish

Résumé

R2TP is a highly conserved chaperone complex formed by two AAA+ ATPases, RUVBL1 and RUVBL2, that associate with PIH1D1 and RPAP3 proteins. R2TP acts in promoting macromolecular complex formation. Here, we establish the principles of R2TP assembly. Three distinct RUVBL1/2-based complexes are identified: R2TP, RUVBL1/2-RPAP3 (R2T), and RUVBL1/2-PIH1D1 (R2P). Interestingly, we find that PIH1D1 does not bind to RUVBL1/RUVBL2 in R2TP and does not function as a nucleotide exchange factor; instead, RPAP3 is found to be the central subunit coordinating R2TP architecture and linking PIH1D1 and RUVBL1/2. We also report that RPAP3 contains an intrinsically disordered N-terminal domain mediating interactions with substrates whose sequences are primarily enriched for Armadillo repeat domains and other helical-type domains. Our work provides a clear and consistent model of R2TP complex structure and gives important insights into how a chaperone machine concerned with assembly of folded proteins into multisubunit complexes might work.

Identifiants

DOI: 10.1016/j.str.2021.08.002 PMID: 34492227
pubmed: 34492227
pii: S0969-2126(21)00297-5
doi: 10.1016/j.str.2021.08.002
pii:
doi:

Substances chimiques

Apoptosis Regulatory Proteins 0
Carrier Proteins 0
Multiprotein Complexes 0
PIH1D1 protein, human 0
RPAP3 protein, human 0
ATPases Associated with Diverse Cellular Activities EC 3.6.4.-
DNA Helicases EC 3.6.4.-
RUVBL1 protein, human EC 3.6.4.12
RUVBL2 protein, human EC 3.6.4.12

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

156-171.e12

Subventions

Organisme : CIHR
ID : 396113
Pays : Canada
Organisme : CIHR
ID : PJT-173491
Pays : Canada
Organisme : CIHR
ID : FDN-154318
Pays : Canada

Informations de copyright

Copyright © 2021 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of interests The authors declare no competing interests. P.K. is a founder, director, and shareholder in Refeyn Ltd. G.Y. is a founder, consultant, and shareholder in Refeyn Ltd.

Auteurs

Thiago V Seraphim (TV)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada; Department of Chemistry and Biochemistry, University of Regina, Regina, SK S4S 0A2, Canada.

Nardin Nano (N)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada.

Yiu Wing Sunny Cheung (YWS)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada.

Siripat Aluksanasuwan (S)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada; Medical Proteomics Unit, Office for Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand.

Carolina Colleti (C)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada; Center of Biological and Health Sciences, Federal University of São Carlos, São Carlos, SP 13560-970, Brazil.

Yu-Qian Mao (YQ)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada.

Vaibhav Bhandari (V)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada.

Gavin Young (G)

Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK.

Larissa Höll (L)

Department of Chemistry and Biochemistry, University of Regina, Regina, SK S4S 0A2, Canada.

Sadhna Phanse (S)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada; Department of Chemistry and Biochemistry, University of Regina, Regina, SK S4S 0A2, Canada.

Yuliya Gordiyenko (Y)

Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK.

Daniel R Southworth (DR)

Department of Biochemistry and Biophysics, Institute for Neurodegenerative Diseases, University of California, San Francisco, CA 94158, USA.

Carol V Robinson (CV)

Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK.

Visith Thongboonkerd (V)

Medical Proteomics Unit, Office for Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand.

Lisandra M Gava (LM)

Center of Biological and Health Sciences, Federal University of São Carlos, São Carlos, SP 13560-970, Brazil.

Júlio C Borges (JC)

São Carlos Institute of Chemistry, University of São Paulo, São Carlos, SP 13566-590, Brazil.

Mohan Babu (M)

Department of Chemistry and Biochemistry, University of Regina, Regina, SK S4S 0A2, Canada.

Leandro R S Barbosa (LRS)

Institute of Physics, University of São Paulo, São Paulo, SP 05508-090, Brazil; Brazilian Synchrotron Light Laboratory (LNLS), Brazilian Center for Research in Energy and Materials (CNPEM), Campinas, SP 13083-100, Brazil.

Carlos H I Ramos (CHI)

Institute of Chemistry, University of Campinas (UNICAMP), Campinas, SP 13083-970, Brazil.

Philipp Kukura (P)

Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK.

Walid A Houry (WA)

Department of Biochemistry, University of Toronto, 661 University Avenue, MaRS Centre, West Tower, Room 1612, Toronto, ON M5G 1M1, Canada; Department of Chemistry, University of Toronto, Toronto, ON M5S 3H6, Canada. Electronic address: walid.houry@utoronto.ca.

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Classifications MeSH

questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Protéines AAA › ATPases associated with diverse cellular activities › Assembly principles of the human R2TP...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines et peptides de signalisation intracellulaire › Protéines régulatrices de l'apoptose › Assembly principles of the human R2TP...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Sites de fixation › Assembly principles of the human R2TP...
questionsmedicales.fr › Acides aminés, peptides et protéines › Protéines › Protéines de transport › Assembly principles of the human R2TP...
questionsmedicales.fr › Techniques d'investigation › Techniques de chimie analytique › Chromatographie › Chromatographie en phase liquide › Chromatographie sur gel › Assembly principles of the human R2TP...
questionsmedicales.fr › Enzymes et coenzymes › Enzymes › Isomerases › Helicase › Assembly principles of the human R2TP...
questionsmedicales.fr › Eucaryotes › Animaux › Chordés › Vertébrés › Mammifères › Eutheria › Primates › Haplorhini › Catarrhini › Hominidae › Humains › Assembly principles of the human R2TP...
questionsmedicales.fr › Techniques d'investigation › Modèles théoriques › Modèles moléculaires › Assembly principles of the human R2TP...
questionsmedicales.fr › Structures macromoléculaires › Complexes multiprotéiques › Assembly principles of the human R2TP...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Assembly principles of the human R2TP...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure tertiaire des protéines › Domaines protéiques › Assembly principles of the human R2TP...
questionsmedicales.fr › Phénomènes chimiques › Phénomènes biochimiques › Conformation moléculaire › Conformation des protéines › Structure quaternaire des protéines › Assembly principles of the human R2TP...