ATP6 Homoplasmic Mutations Inhibit and Destabilize the Human F1F0-ATP Synthase without Preventing Enzyme Assembly and Oligomerization
نویسندگان
چکیده
منابع مشابه
Structure of dimeric F1F0-ATP synthase.
The structure of the dimeric ATP synthase from yeast mitochondria was analyzed by transmission electron microscopy and single particle image analysis. In addition to the previously reported side views of the dimer, top view and intermediate projections served to resolve the arrangement of the rotary c(10) ring and the other stator subunits at the F(0)-F(0) dimeric interface. A three-dimensional...
متن کاملATP synthesis driven by proton transport in F1F0-ATP synthase.
Topical questions in ATP synthase research are: (1) how do protons cause subunit rotation and how does rotation generate ATP synthesis from ADP+Pi? (2) How does hydrolysis of ATP generate subunit rotation and how does rotation bring about uphill transport of protons? The finding that ATP synthase is not just an enzyme but rather a unique nanomotor is attracting a diverse group of researchers ke...
متن کاملCharacterization of mutations in the b subunit of F1F0 ATP synthase in Escherichia coli.
Site-directed mutagenesis was used to investigate the restrictions on Ala-79 of the b subunit in F1F0 adenosine triphosphate synthase. This amino acid had been previously identified as particularly sensitive to mutation (McCormick, K. A., and Cain, B. D. (1991) J. Bacteriol. 173, 7240-7248). Mutant uncF (b) genes were placed under control of the lac promoter and monitored for F1F0 ATP synthase ...
متن کاملThe Escherichia coli F1F0 ATP synthase displays biphasic synthesis kinetics.
The F1F0 proton-translocating ATPase/synthase is the primary generator of ATP in most organisms growing aerobically. Kinetic assays of ATP synthesis have been conducted using enzymes from mitochondria and chloroplasts. However, limited data on ATP synthesis by the model Escherichia coli enzyme are available, mostly because of the lack of an efficient and reproducible assay. We have developed an...
متن کاملHuman F1F0 ATP Synthase, Mitochondrial Ultrastructure and OXPHOS Impairment: A (Super-)Complex Matter?
Mitochondrial morphogenesis is a key process of cell physiology. It is essential for the proper function of this double membrane-delimited organelle, as it ensures the packing of the inner membrane in a very ordered pattern called cristae. In yeast, the mitochondrial ATP synthase is able to form dimers that can assemble into oligomers. Two subunits (e and g) are involved in this supramolecular ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2007
ISSN: 0021-9258
DOI: 10.1074/jbc.m606828200