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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

ssembly principles of the human R2TP chaperone complex reveal the presence of R2T and R2P complexe

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Author(s):
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Seraphim, V, Thiago ; Nano, Nardin [1] ; Cheung, Yiu Wing Sunny [1] ; Aluksanasuwan, Siripat [1, 2, 3] ; Colleti, Carolina [4, 1] ; Mao, Yu-Qian [1] ; Bhandari, Vaibhav [1] ; Young, Gavin [5] ; Holl, Larissa [6] ; Phanse, Sadhna [1, 6] ; Gordiyenko, Yuliya [5] ; Southworth, Daniel R. [7] ; Robinson, V, Carol ; Thongboonkerd, Visith [2] ; Gava, Lisandra M. [4] ; Borges, Julio C. [8] ; Babu, Mohan [6] ; Barbosa, Leandro R. S. [9, 10] ; Ramos, I, Carlos H. ; Kukura, Philipp [11] ; Houry, Walid A. [12, 1]
Total Authors: 21
Affiliation:
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[1] Seraphim, Thiago, V, Univ Toronto, Dept Biochem, MaRS Ctr, 661 Univ Ave, West Tower, Room 1612, Toronto, ON M5G 1M1 - Canada
[2] Mahidol Univ, Fac Med Siriraj Hosp, Med Prote Unit, Off Res & Dev, Bangkok - Thailand
[3] Mae Fah Luang Univ, Sch Med, Chiang Rai - Thailand
[4] Univ Fed Sao Carlos, Ctr Biol & Hlth Sci, BR-13560970 Sao Carlos, SP - Brazil
[5] Univ Oxford, Dept Chem, Phys & Theoret Chem Lab, Oxford OX1 3QZ - England
[6] Seraphim, Thiago, V, Univ Regina, Dept Chem & Biochem, Regina, SK S4S 0A2 - Canada
[7] Univ Calif San Francisco, Dept Biochem & Biophys, Inst Neurodegenerat Dis, San Francisco, CA 94158 - USA
[8] Univ Sao Paulo, Sao Carlos Inst Chem, BR-13566590 Sao Carlos, SP - Brazil
[9] Univ Sao Paulo, Inst Phys, BR-05508090 Sao Paulo, SP - Brazil
[10] Brazilian Ctr Res Energy & Mat CNPEM, Brazilian Synchrotron Light Lab LNLS, BR-13083100 Campinas, SP - Brazil
[11] Robinson, Carol, V, Univ Oxford, Dept Chem, Phys & Theoret Chem Lab, Oxford OX1 3QZ - England
[12] Univ Toronto, Dept Chem, Toronto, ON M5S 3H6 - Canada
Total Affiliations: 12
Document type: Journal article
Source: Structure; v. 30, n. 1, p. 156+, JAN 6 2022.
Web of Science Citations: 0
Abstract

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. (AU)

FAPESP's process: 17/26131-5 - The chaperome: study of the relationship of the structure of its components and the maintenance of proteostasis
Grantee:Carlos Henrique Inacio Ramos
Support type: Research Projects - Thematic Grants
FAPESP's process: 12/50161-8 - Study of the structure and function of the Hsp90 chaperone with emphasis on its role in cellular homeostasis
Grantee:Carlos Henrique Inacio Ramos
Support type: Research Projects - Thematic Grants
FAPESP's process: 15/15822-1 - Physicochemical and structural properties of Ionic Liquids and drugs interacting with biologicaly relevant systems.
Grantee:Leandro Ramos Souza Barbosa
Support type: Regular Research Grants
FAPESP's process: 16/05019-0 - The thermodynamical and structural influence of ionic liquids in biomimetic membrane models
Grantee:Natália Fernandes de Oliveira
Support type: Scholarships in Brazil - Scientific Initiation
FAPESP's process: 16/01603-9 - Determining physical interactions required for R2TP complex assembly using biophysical and biochemical approaches
Grantee:Carolina Colleti
Support type: Scholarships abroad - Research Internship - Scientific Initiation
FAPESP's process: 12/01953-9 - Proteins under fibrillation process: a structural and spectroscopic study of the influence of denaturating agents
Grantee:Leandro Ramos Souza Barbosa
Support type: Regular Research Grants