Accessible Requires Authentication Published by De Gruyter April 1, 2015

Hybrid rotors in F1Fo ATP synthases: subunit composition, distribution, and physiological significance

Karsten Brandt and Volker Müller
From the journal Biological Chemistry

Abstract

The c ring of the Na+ F1Fo ATP synthase from the anaerobic acetogenic bacterium Acetobacterium woodii is encoded by three different genes: atpE1, atpE2 and atpE3. Subunit c1 is similar to typical V-type c subunits and has four transmembrane helices with one ion binding site. Subunit c2 and c3 are identical at the amino acid level and are typical F-type c subunits with one ion binding site in two transmembrane helices. All three constitute a hybrid FoVoc ring, the first found in nature. To analyze whether other species may have similar hybrid rotors, we searched every genome sequence publicly available as of 23 February 2015 for F1Fo ATPase operons that have more than one gene encoding the c subunit. This revealed no other species that has three different c subunit encoding genes but twelve species that encode one Fo- and one Vo-type c subunit in one operon. Their c subunits have the conserved binding motif for Na+. The organisms are all anaerobic. The advantage of hybrid c rings for the organisms in their environments is discussed.


Corresponding author: Volker Müller, Molecular Microbiology and Bioenergetics, Institute of Molecular Biosciences, Johann Wolfgang Goethe University Frankfurt, Max-von-Laue-Str. 9, D-60438 Frankfurt/Main, Germany, e-mail:

Acknowledgments

This work was supported by grants from the Deutsche Forschungsgemeinschaft (SFB 807).

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Received: 2015-3-2
Accepted: 2015-3-25
Published Online: 2015-4-1
Published in Print: 2015-9-1

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