The regulatory subunit ε in Escherichia coli FOF1-ATP synthase.

@article{Sielaff2018TheRS,
  title={The regulatory subunit $\epsilon$ in Escherichia coli FOF1-ATP synthase.},
  author={Hendrik Sielaff and Thomas M. Duncan and Michael B{\"o}rsch},
  journal={Biochimica et biophysica acta. Bioenergetics},
  year={2018},
  volume={1859 9},
  pages={
          775-788
        }
}

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References

SHOWING 1-10 OF 197 REFERENCES
Regulatory conformational changes of the Ɛ subunit in single FRET-labeled F0F1-ATP synthase
TLDR
An experimental system is developed that can reveal conditions under which ε inhibits the holoenzyme FoF1-ATP synthase in vitro and labels the C-terminal domain of ε and the γ subunit specifically with two different fluorophores for single-molecule Förster resonance energy transfer (smFRET).
Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data
TLDR
It is concluded that the ɛ subunit from the bacterial F-type ATP synthases is indeed capable of regulating ATP hydrolysis activity in a wide variety of bacteria, making it a potentially valuable drug target, but its exact role is still under debate.
Rotor/Stator Interactions of the ϵ Subunit in Escherichia coli ATP Synthase and Implications for Enzyme Regulation*
TLDR
Disulfide cross-linking of substituted cysteines on functionally coupled ATP synthase is used to characterize interactions of ϵ with an F0 component of the rotor (subunit c) and with an C-terminal domain of the stator ( subunit β) to demonstrate the ability ofπ to span the central stalk region from the surface of the membrane (ϵ-c) to the bottom of F1 (β-ϵ).
Structure of the ATP synthase catalytic complex (F1) from Escherichia coli in an auto-inhibited conformation
TLDR
The crystal structure of the ATP synthase catalytic complex (F1) from Escherichia coli described here reveals the structural basis for autoinhibition by one of its rotary stalk subunits, and adopts a heretofore unknown, highly extended conformation that inserts deeply into the central cavity of the enzyme.
Deleting the IF1-like ζ subunit from Paracoccus denitrificans ATP synthase is not sufficient to activate ATP hydrolysis
TLDR
De deleting the P. denitrificans ζ subunit is not sufficient to activate ATP hydrolysis, and the rate of ATP Hydrolysis increased by less than twofold, remaining negligible in comparison with the rates of the Escherichia coli and mammalian enzymes.
Chemomechanical coupling of human mitochondrial F1-ATPase motor.
TLDR
ATP-driven rotation of human mitochondrial F1 is reported, demonstrating that chemomechanical coupling angles of the γ-subunit are tuned during evolution.
Structures of the thermophilic F1-ATPase ε subunit suggesting ATP-regulated arm motion of its C-terminal domain in F1
TLDR
It is suggested that the ε C-terminal domain can undergo an arm-like motion in response to an ATP concentration change and thereby contribute to regulation of FoF1-ATP synthase.
The ATP synthase: the understood, the uncertain and the unknown.
  • J. Walker
  • Biology
    Biochemical Society transactions
  • 2013
TLDR
Evidence is growing for other roles of ATP synthases in the inner membranes of mitochondria, where they form supermolecular complexes, possibly with specific lipids, and these complexes probably contribute to, or even determine, the formation of the cristae.
Rotation and structure of FoF1-ATP synthase.
TLDR
A review summarizes the latest findings about the two motors of F(o)F(1)-ATP synthase as well as a brief historical background, which indicates that this enzyme operates on the nanometre scale and works with extremely high efficiency.
Regulatory Interplay between Proton Motive Force, ADP, Phosphate, and Subunit ϵ in Bacterial ATP Synthase*
TLDR
The C-terminal domain of subunit ϵ in the Bacillus PS3 enzyme enhanced ADP inhibition by counteracting the effects of pmf, allowing the enzyme to promptly respond to changes in the ATP:ADP ratio and in pmf levels in order to avoid potentially wasteful ATP hydrolysis in vivo.
...
...