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Journal Article
Modular assembly of yeast mitochondrial ATP synthase
2011
Overview
The mitochondrial ATP synthase (F
1
–F
0
complex) of
Saccharomces cerevisiae
is a composite of different structural and functional units that jointly couple ATP synthesis and hydrolysis to proton transfer across the inner membrane.
In organello
, pulse labelling and pulse‐chase experiments have enabled us to track the mitochondrially encoded Atp6p, Atp8p and Atp9p subunits of F
0
and to identify different assembly intermediates into which they are assimilated. Surprisingly, these core subunits of F
0
segregated into two different assembly intermediates one of which is composed of Atp6p, Atp8p, at least two stator subunits, and the Atp10p chaperone while the second consists of the F
1
ATPase and Atp9p ring. These studies show that assembly of the ATP synthase is not a single linear process, as previously thought, but rather involves two separate but coordinately regulated pathways that converge at the end stage.
The assembly of the mitochondrial F
1
–F
O
ATP synthase complex involves two separate assembly intermediates, an Atp6p/Atp8p complex and the Atp9p ring in complex with the F
1
sector.
Publisher
John Wiley & Sons, Ltd,Nature Publishing Group UK,Springer Nature B.V,Nature Publishing Group
Subject
/ ATPase
/ DNA, Mitochondrial - genetics
/ DNA, Mitochondrial - metabolism
/ Enzymes
/ Mitochondrial Proton-Translocating ATPases - chemistry
/ Mitochondrial Proton-Translocating ATPases - genetics
/ Mitochondrial Proton-Translocating ATPases - metabolism
/ Proton-Translocating ATPases - genetics
/ Proton-Translocating ATPases - metabolism
/ Saccharomyces cerevisiae - genetics
/ Saccharomyces cerevisiae - growth & development
/ Saccharomyces cerevisiae - metabolism
/ Saccharomyces cerevisiae Proteins - genetics
/ Saccharomyces cerevisiae Proteins - metabolism
/ Yeast
/ Yeasts
