The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase

The mitochondrial F(1)F(O)-ATP synthase produces the bulk of cellular ATP. The soluble F(1) domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the F(O) domain. The assembly of the F(1) domain and its linkage to the perip...

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Autores principales: Song, Jiyao, Steidle, Liesa, Steymans, Isabelle, Singh, Jasjot, Sanner, Anne, Böttinger, Lena, Winter, Dominic, Becker, Thomas
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
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Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9810599/
https://www.ncbi.nlm.nih.gov/pubmed/36596815
http://dx.doi.org/10.1038/s41467-022-35720-5
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author Song, Jiyao
Steidle, Liesa
Steymans, Isabelle
Singh, Jasjot
Sanner, Anne
Böttinger, Lena
Winter, Dominic
Becker, Thomas
author_facet Song, Jiyao
Steidle, Liesa
Steymans, Isabelle
Singh, Jasjot
Sanner, Anne
Böttinger, Lena
Winter, Dominic
Becker, Thomas
author_sort Song, Jiyao
collection PubMed
description The mitochondrial F(1)F(O)-ATP synthase produces the bulk of cellular ATP. The soluble F(1) domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the F(O) domain. The assembly of the F(1) domain and its linkage to the peripheral stalk is poorly understood. Here we show a dual function of the mitochondrial Hsp70 (mtHsp70) in the formation of the ATP synthase. First, it cooperates with the assembly factors Atp11 and Atp12 to form the F(1) domain of the ATP synthase. Second, the chaperone transfers Atp5 into the assembly line to link the catalytic head with the peripheral stalk. Inactivation of mtHsp70 leads to integration of assembly-defective Atp5 variants into the mature complex, reflecting a quality control function of the chaperone. Thus, mtHsp70 acts as an assembly and quality control factor in the biogenesis of the F(1)F(O)-ATP synthase.
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spelling pubmed-98105992023-01-05 The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase Song, Jiyao Steidle, Liesa Steymans, Isabelle Singh, Jasjot Sanner, Anne Böttinger, Lena Winter, Dominic Becker, Thomas Nat Commun Article The mitochondrial F(1)F(O)-ATP synthase produces the bulk of cellular ATP. The soluble F(1) domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the F(O) domain. The assembly of the F(1) domain and its linkage to the peripheral stalk is poorly understood. Here we show a dual function of the mitochondrial Hsp70 (mtHsp70) in the formation of the ATP synthase. First, it cooperates with the assembly factors Atp11 and Atp12 to form the F(1) domain of the ATP synthase. Second, the chaperone transfers Atp5 into the assembly line to link the catalytic head with the peripheral stalk. Inactivation of mtHsp70 leads to integration of assembly-defective Atp5 variants into the mature complex, reflecting a quality control function of the chaperone. Thus, mtHsp70 acts as an assembly and quality control factor in the biogenesis of the F(1)F(O)-ATP synthase. Nature Publishing Group UK 2023-01-03 /pmc/articles/PMC9810599/ /pubmed/36596815 http://dx.doi.org/10.1038/s41467-022-35720-5 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
Song, Jiyao
Steidle, Liesa
Steymans, Isabelle
Singh, Jasjot
Sanner, Anne
Böttinger, Lena
Winter, Dominic
Becker, Thomas
The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase
title The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase
title_full The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase
title_fullStr The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase
title_full_unstemmed The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase
title_short The mitochondrial Hsp70 controls the assembly of the F(1)F(O)-ATP synthase
title_sort mitochondrial hsp70 controls the assembly of the f(1)f(o)-atp synthase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9810599/
https://www.ncbi.nlm.nih.gov/pubmed/36596815
http://dx.doi.org/10.1038/s41467-022-35720-5
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