ATP synthase subunit c/III/9 gene sequences as a tool for interkingdom and metaphytes molecular phylogenies

1992 ◽  
Vol 34 (4) ◽  
pp. 292-303 ◽  
Author(s):  
Herv� Recipon ◽  
Roland Perasso ◽  
Andr� Adoutte ◽  
Francis Quetier
Keyword(s):  
Atp Synthase ◽  
Gene Sequences ◽  
Subunit C ◽  
Molecular Phylogenies

scholarly journals Lysine methylation of mitochondrial ATP synthase subunit c stored in tissues of dogs with hereditary ceroid lipofuscinosis

1994 ◽  
Vol 269 (13) ◽  
pp. 9906-9911
Author(s):  
M.L. Katz ◽  
J.S. Christianson ◽  
N.E. Norbury ◽  
C.L. Gao ◽  
A.N. Siakotos ◽  
...  
Keyword(s):  
Atp Synthase ◽  
Lysine Methylation ◽  
Subunit C ◽  
Ceroid Lipofuscinosis ◽  
Mitochondrial Atp Synthase

scholarly journals Crystallographic structure of the turbine C-ring from spinach chloroplast F-ATP synthase

2014 ◽  
Vol 34 (2) ◽  
Author(s):  
Asha Manikkoth Balakrishna ◽  
Holger Seelert ◽  
Sven-Hendric Marx ◽  
Norbert A. Dencher ◽  
Gerhard Grüber
Keyword(s):  
Atp Synthase ◽  
Ring Width ◽  
Atp Synthesis ◽  
Crystallographic Structure ◽  
Unit Cell Parameters ◽  
Subunit C ◽  
Cell Parameters ◽  
Ring Diameter ◽  
C Subunit

In eukaryotic and prokaryotic cells, F-ATP synthases provide energy through the synthesis of ATP. The chloroplast F-ATP synthase (CF1FO-ATP synthase) of plants is integrated into the thylakoid membrane via its FO-domain subunits a, b, b’ and c. Subunit c with a stoichiometry of 14 and subunit a form the gate for H+-pumping, enabling the coupling of electrochemical energy with ATP synthesis in the F1 sector. Here we report the crystallization and structure determination of the c14-ring of subunit c of the CF1FO-ATP synthase from spinach chloroplasts. The crystals belonged to space group C2, with unit-cell parameters a=144.420, b=99.295, c=123.51 Å, and β=104.34° and diffracted to 4.5 Å resolution. Each c-ring contains 14 monomers in the asymmetric unit. The length of the c-ring is 60.32 Å, with an outer ring diameter 52.30 Å and an inner ring width of 40 Å.

Biological-to-electronic interface with pores of ATP synthase subunit C in silicon nitride barrier

2000 ◽  
Vol 38 (1) ◽  
pp. 113-119 ◽  
Author(s):  
J. E. M. McGeoch ◽  
M. W. McGeoch ◽  
D. J. D. Carter ◽  
R. F. Shuman ◽  
G. Guidotti
Keyword(s):  
Silicon Nitride ◽  
Atp Synthase ◽  
Subunit C ◽  
Electronic Interface

scholarly journals Reversible Thiol Oxidation Inhibits the Mitochondrial ATP Synthase in Xenopus laevis Oocytes

Antioxidants ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 215 ◽  
Author(s):  
James Cobley ◽  
Anna Noble ◽  
Rachel Bessell ◽  
Matthew Guille ◽  
Holger Husi
Keyword(s):  
Xenopus Laevis ◽  
Atp Synthase ◽  
Xenopus Laevis Oocytes ◽  
Proton Pumps ◽  
Thiol Oxidation ◽  
Protein Thiol ◽  
Complex Iv ◽  
Subunit C ◽  
Catalyst Free ◽  
Mitochondrial Atp Synthase

Oocytes are postulated to repress the proton pumps (e.g., complex IV) and ATP synthase to safeguard mitochondrial DNA homoplasmy by curtailing superoxide production. Whether the ATP synthase is inhibited is, however, unknown. Here we show that: oligomycin sensitive ATP synthase activity is significantly greater (~170 vs. 20 nmol/min−1/mg−1) in testes compared to oocytes in Xenopus laevis (X. laevis). Since ATP synthase activity is redox regulated, we explored a regulatory role for reversible thiol oxidation. If a protein thiol inhibits the ATP synthase, then constituent subunits must be reversibly oxidised. Catalyst-free trans-cyclooctene 6-methyltetrazine (TCO-Tz) immunocapture coupled to redox affinity blotting reveals several subunits in F1 (e.g., ATP-α-F1) and Fo (e.g., subunit c) are reversibly oxidised. Catalyst-free TCO-Tz Click PEGylation reveals significant (~60%) reversible ATP-α-F1 oxidation at two evolutionary conserved cysteine residues (C244 and C294) in oocytes. TCO-Tz Click PEGylation reveals ~20% of the total thiols in the ATP synthase are substantially oxidised. Chemically reversing thiol oxidation significantly increased oligomycin sensitive ATP synthase activity from ~12 to 100 nmol/min−1/mg−1 in oocytes. We conclude that reversible thiol oxidation inhibits the mitochondrial ATP synthase in X. laevis oocytes.

Orientation of subunit c of the ATP synthase of Escherichia coli — a study with peptide-specific antibodies

1990 ◽  
Vol 1016 (1) ◽  
pp. 63-70 ◽  
Author(s):  
Michael Hensel ◽  
Gabriele Deckers-Hebestreit ◽  
Roland Schmid ◽  
Karlheinz Altendorf
Keyword(s):  
Escherichia Coli ◽  
Atp Synthase ◽  
Subunit C ◽  
Specific Antibodies

Evolution of ATP synthase subunit c and cytochrome c gene families in selected Metazoan classes

Gene ◽  
2006 ◽  
Vol 371 (2) ◽  
pp. 224-233 ◽  
Author(s):  
Anna De Grassi ◽  
Cecilia Lanave ◽  
Cecilia Saccone
Keyword(s):  
Cytochrome C ◽  
Atp Synthase ◽  
Gene Families ◽  
Subunit C
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