F<inf>o</inf>-driven rotation in the ATP synthase direction against the force of F<inf>1</inf> ATPase in the F<inf>o</inf>F<inf>1</inf> ATP lynthase

James Martin, Jennifer Hudson, Tassilo Hornung, Wayne Frasch

Research output: Contribution to journalArticle

9 Scopus citations

Abstract

Living organisms rely on the F<inf>o</inf>F<inf>1</inf> 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 F<inf>o</inf> motor uses a transmembrane electrochemical ion gradient to create clockwise torque that overcomes F<inf>1</inf> ATPase-driven counterclockwise torque at high ATP is a major unresolved question. Using single F<inf>o</inf>F<inf>1</inf> molecules embedded in lipid bilayer nanodiscs, we now report the observation of F<inf>o</inf>-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 F<inf>o</inf> 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

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ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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