The mitochondrial Hsp70 controls the assembly of the F1FO-ATP synthase

Jiyao Song, Liesa Steidle, Isabelle Steymans, Jasjot Singh, Anne Sanner, Lena Böttinger, Dominic Winter and Thomas Becker ()
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Jiyao Song: University of Bonn
Liesa Steidle: University of Freiburg
Isabelle Steymans: University of Bonn
Jasjot Singh: University of Bonn
Anne Sanner: University of Bonn
Lena Böttinger: University of Freiburg
Dominic Winter: University of Bonn
Thomas Becker: University of Bonn

Nature Communications, 2023, vol. 14, issue 1, 1-15

Abstract: Abstract The mitochondrial F1FO-ATP synthase produces the bulk of cellular ATP. The soluble F1 domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the FO domain. The assembly of the F1 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 F1 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 F1FO-ATP synthase.

Date: 2023
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DOI: 10.1038/s41467-022-35720-5

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