Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12

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Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12. / Weinhäupl, Katharina; Wang, Yong; Hessel, Audrey; Brennich, Martha; Lindorff-Larsen, Kresten; Schanda, Paul.

I: Structure, Bind 29, Nr. 9, 2021, s. 1065-1073.e4.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Weinhäupl, K, Wang, Y, Hessel, A, Brennich, M, Lindorff-Larsen, K & Schanda, P 2021, 'Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12', Structure, bind 29, nr. 9, s. 1065-1073.e4. https://doi.org/10.1016/j.str.2021.04.009

APA

Weinhäupl, K., Wang, Y., Hessel, A., Brennich, M., Lindorff-Larsen, K., & Schanda, P. (2021). Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12. Structure, 29(9), 1065-1073.e4. https://doi.org/10.1016/j.str.2021.04.009

Vancouver

Weinhäupl K, Wang Y, Hessel A, Brennich M, Lindorff-Larsen K, Schanda P. Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12. Structure. 2021;29(9):1065-1073.e4. https://doi.org/10.1016/j.str.2021.04.009

Author

Weinhäupl, Katharina ; Wang, Yong ; Hessel, Audrey ; Brennich, Martha ; Lindorff-Larsen, Kresten ; Schanda, Paul. / Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12. I: Structure. 2021 ; Bind 29, Nr. 9. s. 1065-1073.e4.

Bibtex

@article{7d172bea33da46feba93034973400423,
title = "Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12",
abstract = "Tim chaperones transport membrane proteins to the two mitochondrial membranes. TIM9·10, a 70 kDa protein complex formed by 3 copies of Tim9 and Tim10, guides its clients across the aqueous compartment. The TIM9·10·12 complex is the anchor point at the inner-membrane insertase TIM22. The subunit composition of TIM9·10·12 remains debated. Joint NMR, small-angle X-ray scattering, and MD simulation data allow us to derive a structural model of the TIM9·10·12 assembly, with a 2:3:1 stoichiometry (Tim9:Tim10:Tim12). Both TIM9·10 and TIM9·10·12 hexamers are in a dynamic equilibrium with their constituent subunits, exchanging on a minutes timescale. NMR data establish that the subunits exhibit large conformational dynamics: when the conserved cysteines of the CX3C-Xn-CX3C motifs are formed, short α helices are formed, and these are fully stabilized only upon formation of the mature hexameric chaperone. We propose that the continuous subunit exchange allows mitochondria to control their level of inter-membrane space chaperones.",
keywords = "kinetics, mitochondrial biogenesis, molecular dynamics simulations, NMR spectroscopy, protein import, real-time NMR, small-angle X-ray scattering, subunit exchange, TIM9·10, TIM9·10·12",
author = "Katharina Weinh{\"a}upl and Yong Wang and Audrey Hessel and Martha Brennich and Kresten Lindorff-Larsen and Paul Schanda",
note = "Publisher Copyright: {\textcopyright} 2021 Elsevier Ltd",
year = "2021",
doi = "10.1016/j.str.2021.04.009",
language = "English",
volume = "29",
pages = "1065--1073.e4",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "9",

}

RIS

TY - JOUR

T1 - Architecture and assembly dynamics of the essential mitochondrial chaperone complex TIM9·10·12

AU - Weinhäupl, Katharina

AU - Wang, Yong

AU - Hessel, Audrey

AU - Brennich, Martha

AU - Lindorff-Larsen, Kresten

AU - Schanda, Paul

N1 - Publisher Copyright: © 2021 Elsevier Ltd

PY - 2021

Y1 - 2021

N2 - Tim chaperones transport membrane proteins to the two mitochondrial membranes. TIM9·10, a 70 kDa protein complex formed by 3 copies of Tim9 and Tim10, guides its clients across the aqueous compartment. The TIM9·10·12 complex is the anchor point at the inner-membrane insertase TIM22. The subunit composition of TIM9·10·12 remains debated. Joint NMR, small-angle X-ray scattering, and MD simulation data allow us to derive a structural model of the TIM9·10·12 assembly, with a 2:3:1 stoichiometry (Tim9:Tim10:Tim12). Both TIM9·10 and TIM9·10·12 hexamers are in a dynamic equilibrium with their constituent subunits, exchanging on a minutes timescale. NMR data establish that the subunits exhibit large conformational dynamics: when the conserved cysteines of the CX3C-Xn-CX3C motifs are formed, short α helices are formed, and these are fully stabilized only upon formation of the mature hexameric chaperone. We propose that the continuous subunit exchange allows mitochondria to control their level of inter-membrane space chaperones.

AB - Tim chaperones transport membrane proteins to the two mitochondrial membranes. TIM9·10, a 70 kDa protein complex formed by 3 copies of Tim9 and Tim10, guides its clients across the aqueous compartment. The TIM9·10·12 complex is the anchor point at the inner-membrane insertase TIM22. The subunit composition of TIM9·10·12 remains debated. Joint NMR, small-angle X-ray scattering, and MD simulation data allow us to derive a structural model of the TIM9·10·12 assembly, with a 2:3:1 stoichiometry (Tim9:Tim10:Tim12). Both TIM9·10 and TIM9·10·12 hexamers are in a dynamic equilibrium with their constituent subunits, exchanging on a minutes timescale. NMR data establish that the subunits exhibit large conformational dynamics: when the conserved cysteines of the CX3C-Xn-CX3C motifs are formed, short α helices are formed, and these are fully stabilized only upon formation of the mature hexameric chaperone. We propose that the continuous subunit exchange allows mitochondria to control their level of inter-membrane space chaperones.

KW - kinetics

KW - mitochondrial biogenesis

KW - molecular dynamics simulations

KW - NMR spectroscopy

KW - protein import

KW - real-time NMR

KW - small-angle X-ray scattering

KW - subunit exchange

KW - TIM9·10

KW - TIM9·10·12

U2 - 10.1016/j.str.2021.04.009

DO - 10.1016/j.str.2021.04.009

M3 - Journal article

C2 - 33974880

AN - SCOPUS:85113869286

VL - 29

SP - 1065-1073.e4

JO - Structure

JF - Structure

SN - 0969-2126

IS - 9

ER -

ID: 280606948