The regulatory subunit ε in Escherichia coli FF-ATP synthase.

TitleThe regulatory subunit ε in Escherichia coli FF-ATP synthase.
Publication TypeJournal Article
Year of Publication2018
AuthorsSielaff, H, Duncan, TM, Börsch, M
JournalBiochim Biophys Acta Bioenerg
Date Published2018 09
KeywordsAdenosine Triphosphate, Energy Metabolism, Escherichia coli, Escherichia coli Proteins, Protein Subunits, Proton-Translocating ATPases

F-type ATP synthases are extraordinary multisubunit proteins that operate as nanomotors. The Escherichia coli (E. coli) enzyme uses the proton motive force (pmf) across the bacterial plasma membrane to drive rotation of the central rotor subunits within a stator subunit complex. Through this mechanical rotation, the rotor coordinates three nucleotide binding sites that sequentially catalyze the synthesis of ATP. Moreover, the enzyme can hydrolyze ATP to turn the rotor in the opposite direction and generate pmf. The direction of net catalysis, i.e. synthesis or hydrolysis of ATP, depends on the cell's bioenergetic conditions. Different control mechanisms have been found for ATP synthases in mitochondria, chloroplasts and bacteria. This review discusses the auto-inhibitory behavior of subunit ε found in FF-ATP synthases of many bacteria. We focus on E. coli FF-ATP synthase, with insights into the regulatory mechanism of subunit ε arising from structural and biochemical studies complemented by single-molecule microscopy experiments.

Alternate JournalBiochim Biophys Acta Bioenerg
Citation Key10.1016/j.bbabio.2018.06.013
PubMed ID29932911
PubMed Central IDPMC6114093
Grant ListR01 GM083088 / GM / NIGMS NIH HHS / United States