Fo-driven rotation in the ATP synthase direction against the force of F1 ATPase in the FoF1 ATP lynthase

James Martin, Jennifer Hudson, Tassilo Hornung, Wayne Frasch

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Living organisms rely on the FoF1 ATP synthase to maintain the non-equilibrium chemical gradient of ATP to ADP and phosphate that provides the primary energy source for cellular processes. How the Fo motor uses a transmembrane electrochemical ion gradient to create clockwise torque that overcomes F1 ATPase-driven counterclockwise torque at high ATP is a major unresolved question. Using single FoF1 molecules embedded in lipid bilayer nanodiscs, we now report the observation of Fo-dependent rotation of the c10 ring in the ATP synthase (clockwise) direction against the counterclockwise force of ATPase-driven rotation that occurs upon formation of a leash with Fo stator subunit a. Mutational studies indicate that the leash is important for ATP synthase activity and support a mechanism in which residues aGlu-196 and cArg-50 participate in the cytoplasmic proton half-channel to promote leash formation.

Original languageEnglish (US)
Pages (from-to)10717-10728
Number of pages12
JournalJournal of Biological Chemistry
Volume290
Issue number17
DOIs
StatePublished - Apr 24 2015

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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