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ATP synthase: from single molecule to human bioenergetics.

Kagawa Y - Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. (2010)

Bottom Line: F(o)F(1) reconstituted into a lipid membrane is capable of ATP synthesis driven by H(+) flux.As the basic structures of F(1) (alpha(3)beta(3)gammadeltaepsilon) and F(o) (ab(2)c(10)) are ubiquitous, stable thermophilic F(o)F(1) (TF(o)F(1)) has been used to elucidate molecular mechanisms, while human F(1)F(o) (HF(1)F(o)) has been used to study biomedical significance.In contrast to the single operon of TF(o)F(1), HF(o)F(1) is encoded by both nuclear DNA with introns and mitochondrial DNA.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, Tochigi, Japan. kagawa@eiyo.ac.jp

ABSTRACT
ATP synthase (F(o)F(1)) consists of an ATP-driven motor (F(1)) and a H(+)-driven motor (F(o)), which rotate in opposite directions. F(o)F(1) reconstituted into a lipid membrane is capable of ATP synthesis driven by H(+) flux. As the basic structures of F(1) (alpha(3)beta(3)gammadeltaepsilon) and F(o) (ab(2)c(10)) are ubiquitous, stable thermophilic F(o)F(1) (TF(o)F(1)) has been used to elucidate molecular mechanisms, while human F(1)F(o) (HF(1)F(o)) has been used to study biomedical significance. Among F(1)s, only thermophilic F(1) (TF(1)) can be analyzed simultaneously by reconstitution, crystallography, mutagenesis and nanotechnology for torque-driven ATP synthesis using elastic coupling mechanisms. In contrast to the single operon of TF(o)F(1), HF(o)F(1) is encoded by both nuclear DNA with introns and mitochondrial DNA. The regulatory mechanism, tissue specificity and physiopathology of HF(o)F(1) were elucidated by proteomics, RNA interference, cytoplasts and transgenic mice. The ATP synthesized daily by HF(o)F(1) is in the order of tens of kilograms, and is primarily controlled by the brain in response to fluctuations in activity.

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Aligned amino acid sequences12,19) and secondary structure elements71) of α and β subunits in TF1. Solid black lines indicate folds, and these were classified into α-helices (A–H, 1–8) and β-sheets (a–f, 0–8). The labels for folds are provided only for the β subunit, except for the three C-terminal α-helices in the α subunit. Dots indicate every tenth residue. I–XI: areas of αβ contact. Red: catalytic contact areas of β. Pink: catalytic contact areas of α. Blue: non-catalytic contact areas of β. Green: non-catalytic contact areas of α. Colored bars indicate contact residues in TβE. Sequences are divided by red asterisks (*) to indicate the three domains.
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fig04: Aligned amino acid sequences12,19) and secondary structure elements71) of α and β subunits in TF1. Solid black lines indicate folds, and these were classified into α-helices (A–H, 1–8) and β-sheets (a–f, 0–8). The labels for folds are provided only for the β subunit, except for the three C-terminal α-helices in the α subunit. Dots indicate every tenth residue. I–XI: areas of αβ contact. Red: catalytic contact areas of β. Pink: catalytic contact areas of α. Blue: non-catalytic contact areas of β. Green: non-catalytic contact areas of α. Colored bars indicate contact residues in TβE. Sequences are divided by red asterisks (*) to indicate the three domains.

Mentions: Amino acid residues in the different α, β, and γ subunits from TF1,12,19) HF1,21,27,28) BF124) and EF118,65) are aligned19) and expressed in the format α10, which refers to residue #10 in the α subunit. The residue numbers of amino acid sequences in the α and β subunits of TF1 are shown in Fig. 4 (dots indicate every tenth residue).17,19) Primary structures are homologous, with 59% sequence identity between thermophilic α/human α and 68% between thermophilic β/human β.19) The primary structure of the TF1 β subunit showed homology with 270 residues which are identical in the β subunits from HF1, CF1, and EF1.19) The homologies of the amino acid sequence between BF1 and YF1 were 73%, 79% and 40%, respectively, for the α, β and γ subunits.14) As these YF1 subunits were functionally complemented with corresponding BF1 subunits,8) the essential structure is conserved among YF1, BF1 and HF1 (sequence is nearly identical to that of BF1, but there were polymorphisms in HF1).8) Residues forming reverse turns (Gly and Pro) were highly conserved among the β subunits.19) Conserved residues (green and blue letters in Fig. 4) among TF1, HF1 and EF1 are closely related to catalytic and regulatory functions.19,21,65) The observed substitutions in the thermophilic subunit increased its propensities to form secondary structures, and its external polarity to form tertiary structure.19)


ATP synthase: from single molecule to human bioenergetics.

Kagawa Y - Proc. Jpn. Acad., Ser. B, Phys. Biol. Sci. (2010)

Aligned amino acid sequences12,19) and secondary structure elements71) of α and β subunits in TF1. Solid black lines indicate folds, and these were classified into α-helices (A–H, 1–8) and β-sheets (a–f, 0–8). The labels for folds are provided only for the β subunit, except for the three C-terminal α-helices in the α subunit. Dots indicate every tenth residue. I–XI: areas of αβ contact. Red: catalytic contact areas of β. Pink: catalytic contact areas of α. Blue: non-catalytic contact areas of β. Green: non-catalytic contact areas of α. Colored bars indicate contact residues in TβE. Sequences are divided by red asterisks (*) to indicate the three domains.
© Copyright Policy - open-access
Related In: Results  -  Collection

Show All Figures
getmorefigures.php?uid=PMC3066536&req=5

fig04: Aligned amino acid sequences12,19) and secondary structure elements71) of α and β subunits in TF1. Solid black lines indicate folds, and these were classified into α-helices (A–H, 1–8) and β-sheets (a–f, 0–8). The labels for folds are provided only for the β subunit, except for the three C-terminal α-helices in the α subunit. Dots indicate every tenth residue. I–XI: areas of αβ contact. Red: catalytic contact areas of β. Pink: catalytic contact areas of α. Blue: non-catalytic contact areas of β. Green: non-catalytic contact areas of α. Colored bars indicate contact residues in TβE. Sequences are divided by red asterisks (*) to indicate the three domains.
Mentions: Amino acid residues in the different α, β, and γ subunits from TF1,12,19) HF1,21,27,28) BF124) and EF118,65) are aligned19) and expressed in the format α10, which refers to residue #10 in the α subunit. The residue numbers of amino acid sequences in the α and β subunits of TF1 are shown in Fig. 4 (dots indicate every tenth residue).17,19) Primary structures are homologous, with 59% sequence identity between thermophilic α/human α and 68% between thermophilic β/human β.19) The primary structure of the TF1 β subunit showed homology with 270 residues which are identical in the β subunits from HF1, CF1, and EF1.19) The homologies of the amino acid sequence between BF1 and YF1 were 73%, 79% and 40%, respectively, for the α, β and γ subunits.14) As these YF1 subunits were functionally complemented with corresponding BF1 subunits,8) the essential structure is conserved among YF1, BF1 and HF1 (sequence is nearly identical to that of BF1, but there were polymorphisms in HF1).8) Residues forming reverse turns (Gly and Pro) were highly conserved among the β subunits.19) Conserved residues (green and blue letters in Fig. 4) among TF1, HF1 and EF1 are closely related to catalytic and regulatory functions.19,21,65) The observed substitutions in the thermophilic subunit increased its propensities to form secondary structures, and its external polarity to form tertiary structure.19)

Bottom Line: F(o)F(1) reconstituted into a lipid membrane is capable of ATP synthesis driven by H(+) flux.As the basic structures of F(1) (alpha(3)beta(3)gammadeltaepsilon) and F(o) (ab(2)c(10)) are ubiquitous, stable thermophilic F(o)F(1) (TF(o)F(1)) has been used to elucidate molecular mechanisms, while human F(1)F(o) (HF(1)F(o)) has been used to study biomedical significance.In contrast to the single operon of TF(o)F(1), HF(o)F(1) is encoded by both nuclear DNA with introns and mitochondrial DNA.

View Article: PubMed Central - PubMed

Affiliation: Department of Biochemistry, Tochigi, Japan. kagawa@eiyo.ac.jp

ABSTRACT
ATP synthase (F(o)F(1)) consists of an ATP-driven motor (F(1)) and a H(+)-driven motor (F(o)), which rotate in opposite directions. F(o)F(1) reconstituted into a lipid membrane is capable of ATP synthesis driven by H(+) flux. As the basic structures of F(1) (alpha(3)beta(3)gammadeltaepsilon) and F(o) (ab(2)c(10)) are ubiquitous, stable thermophilic F(o)F(1) (TF(o)F(1)) has been used to elucidate molecular mechanisms, while human F(1)F(o) (HF(1)F(o)) has been used to study biomedical significance. Among F(1)s, only thermophilic F(1) (TF(1)) can be analyzed simultaneously by reconstitution, crystallography, mutagenesis and nanotechnology for torque-driven ATP synthesis using elastic coupling mechanisms. In contrast to the single operon of TF(o)F(1), HF(o)F(1) is encoded by both nuclear DNA with introns and mitochondrial DNA. The regulatory mechanism, tissue specificity and physiopathology of HF(o)F(1) were elucidated by proteomics, RNA interference, cytoplasts and transgenic mice. The ATP synthesized daily by HF(o)F(1) is in the order of tens of kilograms, and is primarily controlled by the brain in response to fluctuations in activity.

Show MeSH
Related in: MedlinePlus