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  The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4

Preiss, L., Klyszejko, A. L., Hicks, D. B., Liu, J., Fackelmayer, O. J., Yildiz, Ö., et al. (2013). The c-ring stoichiometry of ATP synthase is adapted to cell physiological requirements of alkaliphilic Bacillus pseudofirmus OF4. Proceedings of the National Academy of Sciences of the United States of America, 110(19), 7874-7879. doi:10.1073/pnas.1303333110.

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 Creators:
Preiss, Laura1, Author           
Klyszejko, Adriana L.1, Author           
Hicks, David B.2, Author
Liu, Jun2, Author
Fackelmayer, Oliver J.2, Author
Yildiz, Özkan1, Author           
Krulwich, Terry A.2, Author
Meier, Thomas1, 3, Author           
Affiliations:
1Department of Structural Biology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068291              
2Pharmacology and Systems Therapeutics, Icahn School of Medicine at Mount Sinai, New York, NY 10029, USA, ou_persistent22              
3Cluster of Excellence Frankfurt Macromolecular Complexes, Goethe University, 60438 Frankfurt am Main, Germany, ou_persistent22              

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Free keywords: F1Fo-ATP synthase rotor; membrane protein complex
 Abstract: The c-rings of ATP synthases consist of individual c-subunits, all of which harbor a conserved motif of repetitive glycine residues (GxGxGxG) important for tight transmembrane α-helix packing. The c-ring stoichiometry determines the number of ions transferred during enzyme operation and has a direct impact on the ion-to-ATP ratio, a cornerstone parameter of cell bioenergetics. In the extreme alkaliphile Bacillus pseudofirmus OF4, the glycine motif is replaced by AxAxAxA. We performed a structural study on two mutants with alanine-to-glycine changes using atomic force microscopy and X-ray crystallography, and found that mutants form smaller c12 rings compared with the WT c13. The molar growth yields of B. pseudofirmus OF4 cells on malate further revealed that the c12 mutants have a considerably reduced capacity to grow on limiting malate at high pH. Our results demonstrate that the mutant ATP synthases with either c12 or c12 can support ATP synthesis, and also underscore the critical importance of an alanine motif with c12 ring stoichiometry for optimal growth at pH >10. The data indicate a direct connection between the precisely adapted ATP synthase c-ring stoichiometry and its ion-to-ATP ratio on cell physiology, and also demonstrate the bioenergetic challenges and evolutionary adaptation strategies of extremophiles.

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Language(s): eng - English
 Dates: 2013-02-222013-04-012013-04-23
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1073/pnas.1303333110
 Degree: -

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Title: Proceedings of the National Academy of Sciences of the United States of America
  Other : PNAS
  Other : Proceedings of the National Academy of Sciences of the USA
  Abbreviation : Proc. Natl. Acad. Sci. U. S. A.
Source Genre: Journal
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Affiliations:
Publ. Info: Washington, D.C. : National Academy of Sciences
Pages: - Volume / Issue: 110 (19) Sequence Number: - Start / End Page: 7874 - 7879 Identifier: ISSN: 0027-8424
CoNE: https://pure.mpg.de/cone/journals/resource/954925427230