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The b Subunit of Escherichia coli ATP Synthase

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Abstract

The b subunit of ATP synthase is a major component of the second stalk connecting the F1and F0 sectors of the enzyme and is essential for normal assembly and function. The156-residue b subunit of the Escherichia coli ATP synthase has been investigated extensivelythrough mutagenesis, deletion analysis, and biophysical characterization. The two copies ofb exist as a highly extended, helical dimer extending from the membrane to near the top ofF1, where they interact with the δ subunit. The sequence has been divided into four domains:the N-terminal membrane-spanning domain, the tether domain, the dimerization domain, andthe C-terminal δ-binding domain. The dimerization domain, contained within residues 60–122,has many properties of a coiled-coil, while the δ-binding domain is more globular. Sites ofcrosslinking between b and the a, α, β, and δ subunits of ATP synthase have been identified,and the functional significance of these interactions is under investigation. The b dimer mayserve as an elastic element during rotational catalysis in the enzyme, but also directly influencesthe catalytic sites, suggesting a more active role in coupling.

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Authors and Affiliations

  1. Department of Biochemistry, University of Western Ontario, London, Ontario, N6A 5C1, Canada

    Stanley D. Dunn

  2. Department of Biochemistry, University of Western Ontario, London, Ontario, N6A 5C1, Canada

    Matthew Revington, Daniel J. Cipriano & Brian H. Shilton

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  1. Stanley D. Dunn
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  3. Daniel J. Cipriano
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  4. Brian H. Shilton
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Dunn, S.D., Revington, M., Cipriano, D.J. et al. The b Subunit of Escherichia coli ATP Synthase . J Bioenerg Biomembr 32, 347–355 (2000). https://doi.org/10.1023/A:1005571818730

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