Proteomics

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

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. We uncovered 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 an assembly-defective Atp5 variant 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.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Saccharomyces Cerevisiae (baker's Yeast)

SUBMITTER: Jasjot Singh  

LAB HEAD: Dominic Winter

PROVIDER: PXD033024 | Pride | 2023-01-11

REPOSITORIES: Pride

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Mit_Library.kit Other
MitoIso_R1.raw Raw
MitoIso_R2.raw Raw
MitoIso_R3.raw Raw
MitoIso_R4.raw Raw
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Publications

The mitochondrial Hsp70 controls the assembly of the F<sub>1</sub>F<sub>O</sub>-ATP synthase.

Song Jiyao J   Steidle Liesa L   Steymans Isabelle I   Singh Jasjot J   Sanner Anne A   Böttinger Lena L   Winter Dominic D   Becker Thomas T  

Nature communications 20230103 1

The mitochondrial F<sub>1</sub>F<sub>O</sub>-ATP synthase produces the bulk of cellular ATP. The soluble F<sub>1</sub> domain contains the catalytic head that is linked via the central stalk and the peripheral stalk to the membrane embedded rotor of the F<sub>O</sub> domain. The assembly of the F<sub>1</sub> 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 coopera  ...[more]

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