DOI: 10.1073/pnas.0706914105. Dodecamer rotor ring defines H <sup>+</sup> /ATP ratio for ATP synthesis of prokaryotic V-ATPase from <i>Thermus thermophilus</i>

Dodecamer rotor ring defines H + /ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus

10.1073/pnas.0706914105

Crossref journal-article

Proceedings of the National Academy of Sciences

Proceedings of the National Academy of Sciences (341)

Abstract

ATP synthesis by V-ATPase from the thermophilic bacterium Thermus thermophilus driven by the acid-base transition was investigated. The rate of ATP synthesis increased in parallel with the increase in proton motive force (PMF) >110 mV, which is composed of a difference in proton concentration (ΔpH) and the electrical potential differences (ΔΨ) across membranes. The optimum rate of synthesis reached 85 s −1 , and the H + /ATP ratio of 4.0 ± 0.1 was obtained. ATP was synthesized at a considerable rate solely by ΔpH, indicating ΔΨ was not absolutely required for synthesis. Consistent with the H + /ATP ratio, cryoelectron micrograph images of 2D crystals of the membrane-bound rotor ring of the V-ATPase at 7.0-Å resolution showed the presence of 12 V o -c subunits, each composed of two transmembrane helices. These results indicate that symmetry mismatch between the rotor and catalytic domains is not obligatory for rotary ATPases/synthases.

Bibliography

Toei, M., Gerle, C., Nakano, M., Tani, K., Gyobu, N., Tamakoshi, M., Sone, N., Yoshida, M., Fujiyoshi, Y., Mitsuoka, K., & Yokoyama, K. (2007). Dodecamer rotor ring defines H + /ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus. Proceedings of the National Academy of Sciences, 104(51), 20256â20261.

Authors 11

Masashi Toei (first)
Christoph Gerle (additional)
Masahiro Nakano (additional)
Kazutoshi Tani (additional)
Nobuhiko Gyobu (additional)
Masatada Tamakoshi (additional)
Nobuhito Sone (additional)
Masasuke Yoshida (additional)
Yoshinori Fujiyoshi (additional)
Kaoru Mitsuoka (additional)
Ken Yokoyama (additional)

References 38 Referenced 79

Dates

Type	When
Created	17 years, 8 months ago (Dec. 11, 2007, 11:47 p.m.)
Deposited	3 years, 4 months ago (April 12, 2022, 4:08 p.m.)
Indexed	4 weeks, 2 days ago (July 24, 2025, 7:41 a.m.)
Issued	17 years, 8 months ago (Dec. 18, 2007)
Published	17 years, 8 months ago (Dec. 18, 2007)
Published Online	17 years, 8 months ago (Dec. 18, 2007)
Published Print	17 years, 8 months ago (Dec. 18, 2007)

Funders 0

None

BibTeX

@article{Toei_2007, title={Dodecamer rotor ring defines H + /ATP ratio for ATP synthesis of prokaryotic V-ATPase from Thermus thermophilus}, volume={104}, ISSN={1091-6490}, url={http://dx.doi.org/10.1073/pnas.0706914105}, DOI={10.1073/pnas.0706914105}, number={51}, journal={Proceedings of the National Academy of Sciences}, publisher={Proceedings of the National Academy of Sciences}, author={Toei, Masashi and Gerle, Christoph and Nakano, Masahiro and Tani, Kazutoshi and Gyobu, Nobuhiko and Tamakoshi, Masatada and Sone, Nobuhito and Yoshida, Masasuke and Fujiyoshi, Yoshinori and Mitsuoka, Kaoru and Yokoyama, Ken}, year={2007}, month=dec, pages={20256–20261} }

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  "abstract": "<jats:p>\n            ATP synthesis by V-ATPase from the thermophilic bacterium\n            <jats:italic>Thermus thermophilus</jats:italic>\n            driven by the acid-base transition was investigated. The rate of ATP synthesis increased in parallel with the increase in proton motive force (PMF) &gt;110 mV, which is composed of a difference in proton concentration (\u0394pH) and the electrical potential differences (\u0394\u03a8) across membranes. The optimum rate of synthesis reached 85 s\n            <jats:sup>\u22121</jats:sup>\n            , and the H\n            <jats:sup>+</jats:sup>\n            /ATP ratio of 4.0 \u00b1 0.1 was obtained. ATP was synthesized at a considerable rate solely by \u0394pH, indicating \u0394\u03a8 was not absolutely required for synthesis. Consistent with the H\n            <jats:sup>+</jats:sup>\n            /ATP ratio, cryoelectron micrograph images of 2D crystals of the membrane-bound rotor ring of the V-ATPase at 7.0-\u212b resolution showed the presence of 12 V\n            <jats:sub>o</jats:sub>\n            -c subunits, each composed of two transmembrane helices. These results indicate that symmetry mismatch between the rotor and catalytic domains is not obligatory for rotary ATPases/synthases.\n          </jats:p>",
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