Cooperation among c-subunits of FoF1-ATP synthase in rotation-coupled proton translocation
Year: 2021
Type: article
Abstract: In F o F 1 -ATP synthase, proton translocation through F o drives rotation of the c -subunit oligomeric ring relative to the a -subunit. Recent studies suggest that in each step of the rotation, key glutamic acid residues in different c -subunits contribute to proton release to and proton uptake from the a -subunit. However, no studies have demonstrated cooperativity among c -subunits toward F o F 1 -ATP synthase activity. Here, we addressed this using Bacillus PS3 ATP synthase harboring a c -ring with various combinations of wild-type and c E56D, enabled by genetically fused single-chain c -ring. ATP synthesis and proton pump activities were decreased by a single c E56D mutation and further decreased by double c E56D mutations. Moreover, activity further decreased as the two mutation sites were separated, indicating cooperation among c -subunits. Similar results were obtained for proton transfer-coupled molecular simulations. The simulations revealed that prolonged proton uptake in mutated c -subunits is shared between two c -subunits, explaining the cooperation observed in biochemical assays.
Source: eLife
DOI: 10.7554/elife.69096
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $2,500
Awards: G242318794, Development of next-generation coarse-grained simulations towards analysis of cellular-scale assembly, Development of practical and effective immersion nanovaccines against bacterial fish diseases using novel nanomaterials, Electrochemical pH control technology in micro/nano space and its bioapplication
OpenAlex ID: W4225752770