The γ‐subunit of ATP synthase from spinach chloroplasts Primary structure deduced from the cloned cDNA sequence

Miki, Junji; Maeda, Masatomo; Mukohata, Yasuo; Futai, Masamitsu

doi:10.1016/0014-5793(88)80421-6

Cited by 152 publications

(75 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Redox-regulation of ATP synthase activity via the g-subunit only occurs in higher plants and green algae (Miki et al, 1988), suggesting that the regulatory mechanism of ATP synthase activity is quite different between cyanobacteria and photosynthetic eukaryotes (Ort and Oxborough, 1992). Based on the structure of CF 1 b, it is clear that the residues in CF 1 b5 are very close to the ADP/ATP binding site.…”

Section: Discussionmentioning

confidence: 99%

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

et al. 2016

View full text Add to dashboard Cite

Thylakoid membrane-localized chloroplast ATP synthases use the proton motive force generated by photosynthetic electron transport to produce ATP from ADP. Although it is well known that the chloroplast ATP synthase is composed of more than 20 proteins with a 3 b 3 g 1 « 1 d 1 I 1 II 1 III 14 IV 1 stoichiometry, its biogenesis process is currently unclear. To unravel the molecular mechanisms underlying the biogenesis of chloroplast ATP synthase, we performed extensive screening for isolating ATP synthase mutants in Arabidopsis (Arabidopsis thaliana). In the recently identified bfa3 (biogenesis factors required for ATP synthase 3) mutant, the levels of chloroplast ATP synthase subunits were reduced to approximately 25% of wild-type levels. In vivo labeling analysis showed that assembly of the CF 1 component of chloroplast ATP synthase was less efficient in bfa3 than in the wild type, indicating that BFA3 is required for CF 1 assembly. BFA3 encodes a chloroplast stromal protein that is conserved in higher plants, green algae, and a few species of other eukaryotic algae, and specifically interacts with the CF 1 b subunit. The BFA3 binding site was mapped to a region in the catalytic site of CF 1 b. Several residues highly conserved in eukaryotic CF 1 b are crucial for the BFA3-CF 1 b interaction, suggesting a coevolutionary relationship between BFA3 and CF 1 b. BFA3 appears to function as a molecular chaperone that transiently associates with unassembled CF 1 b at its catalytic site and facilitates subsequent association with CF 1 a during assembly of the CF 1 subcomplex of chloroplast ATP synthase.

show abstract

Section: Discussionmentioning

confidence: 99%

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

et al. 2016

View full text Add to dashboard Cite

show abstract

“…The conservation of amino acid residues in the Cterminal part of the ␥-subunit (52,53) and in the residues that form the sleeve (25,52), and the effects of mutations in this region of the enzyme in various species (54)(55)(56)(57)(58)(59), provide further support for this view. However, this conclusion seems to be contradicted by experiments on the Escherichia coli, chloroplast, and Bacillus PS3 enzymes, where it has been reported that the C-terminal region ␣-helix of the ␥-subunit can be shortened (by up to 12, 20, and 21 residues, respectively) without effect on catalytic activity (60,61).…”

Section: Mechanism Of Inhibitionmentioning

confidence: 91%

Mechanism of inhibition of bovine F ₁ -ATPase by resveratrol and related polyphenols

Gledhill

Montgomery

Leslie

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

357

330

View full text Add to dashboard Cite

The structures of F1-ATPase from bovine heart mitochondria inhibited with the dietary phytopolyphenol, resveratrol, and with the related polyphenols quercetin and piceatannol have been determined at 2.3-, 2.4-and 2.7-Å resolution, respectively. The inhibitors bind to a common site in the inside surface of an annulus made from loops in the three ␣-and three ␤-subunits beneath the ''crown'' of ␤-strands in their N-terminal domains. This region of F 1-ATPase forms a bearing to allow the rotation of the tip of the ␥-subunit inside the annulus during catalysis. The binding site is a hydrophobic pocket between the C-terminal tip of the ␥-subunit and the ␤TP subunit, and the inhibitors are bound via H-bonds mostly to their hydroxyl moieties mediated by bound water molecules and by hydrophobic interactions. There are no equivalent sites between the ␥-subunit and either the ␤DP or the ␤E subunit. The inhibitors probably prevent both the synthetic and hydrolytic activities of the enzyme by blocking both senses of rotation of the ␥-subunit. The beneficial effects of dietary resveratrol may derive in part by preventing mitochondrial ATP synthesis in tumor cells, thereby inducing apoptosis. mitochondria ͉ oxidative phosphorylation ͉ rotary mechanism ͉ crystal structure

show abstract

“…Alignment of the protein sequences of the y-subunits of ATPases from cyanobacteria [7,8), chloroplasts (c, [6,32]). bacteria [23,25-271 and mitochondria (m, (281).…”

Section: Discussionmentioning

confidence: 99%

“…The total number of amino acids (aa) of the various proteins is given at the end of the sequences. February 1990 [6,32] and Cys-205 which release a cysteine-containing peptide (S2 peptide: -CVDAAEDELFR-, [7,29]). This cysteine, which is not present in the Synechocystis sequence, forms a disulfide bridge with the neighboring Cys-199 in oxidized chloroplast ATPase.…”

Section: Discussionmentioning

confidence: 99%

“…The open reading frame consists of 945 bases which encode a protein of 3 14 amino acids. It shows homologies with both the spinach [6] and the cyanobacterial [7,8] protein sequences, especially at the amino-and carboxyl-terminal ends. In variance to the 4 cysteines found in the spinach y-subunit, only one cysteine residue could be detected in the deduced primary structure of the Synechocystis 6803 protein, in agreement with the two other cyanobacterial y-subunits.…”

Section: Introduction Fofi-atpases (Proton-translocatingmentioning

confidence: 94%

See 1 more Smart Citation

The primary structure of the γ‐subunit of the ATPase from Synechocystis 6803

1990

View full text Add to dashboard Cite

The nucleotide sequence of the gene coding for the F,F,-ATPase y-subunit (arpC) from the transformable cyanobacterium Synechocystis 6083 has been determined. The deduced translation product consists of 314 amino acid residues and is highly homologous (72% identical residues) to the sequences of other cyanobacterial y-subunits. The Synechocystis 6803 sequence is also homologous to the chloroplast y-sequence. Like in the other cyanobacterial subunits, only the first of the 3 cysteine residues, which are involved in energy-linked functions of the y-subunit in spinach chloroplasts, is conserved in Synechocystis 6803.

show abstract

The γ‐subunit of ATP synthase from spinach chloroplasts Primary structure deduced from the cloned cDNA sequence

Cited by 152 publications

References 23 publications

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

Mechanism of inhibition of bovine F ₁ -ATPase by resveratrol and related polyphenols

The primary structure of the γ‐subunit of the ATPase from Synechocystis 6803

Contact Info

Product

Resources

About

The γ‐subunit of ATP synthase from spinach chloroplasts Primary structure deduced from the cloned cDNA sequence

Cited by 152 publications

References 23 publications

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

BIOGENESIS FACTOR REQUIRED FOR ATP SYNTHASE 3 Facilitates Assembly of the Chloroplast ATP Synthase Complex

Mechanism of inhibition of bovine F 1 -ATPase by resveratrol and related polyphenols

The primary structure of the γ‐subunit of the ATPase from Synechocystis 6803

Contact Info

Product

Resources

About

Mechanism of inhibition of bovine F ₁ -ATPase by resveratrol and related polyphenols