Follow-up study of subunit c of mitochondrial ATP synthase (SCMAS) in Batten disease and in unrelated lysosomal disorders

1997 ◽  
Vol 93 (4) ◽  
pp. 379-390 ◽  
Author(s):  
M. Elleder ◽  
J. Sokolová ◽  
M. Hřebíček
Keyword(s):  
Atp Synthase ◽  
Batten Disease ◽  
Subunit C ◽  
Follow Up Study ◽  
Lysosomal Disorders ◽  
Mitochondrial Atp Synthase

scholarly journals Lysine 43 Is Trimethylated in Subunit c from Bovine Mitochondrial ATP Synthase and in Storage Bodies Associated with Batten Disease

2004 ◽  
Vol 279 (21) ◽  
pp. 21883-21887 ◽  
Author(s):  
Ruming Chen ◽  
Ian M. Fearnley ◽  
David N. Palmer ◽  
John E. Walker
Keyword(s):  
Atp Synthase ◽  
Batten Disease ◽  
Subunit C ◽  
Mitochondrial Atp Synthase

Late-infantile Batten disease: Purification of the subunit c of the mitochondrial ATP synthase from storage material

1995 ◽  
Vol 57 (2) ◽  
pp. 272-278 ◽  
Author(s):  
Kevork Hagopian ◽  
Brian D. Lake ◽  
Bryan G. Winchester ◽  
John B. Clark
Keyword(s):  
Atp Synthase ◽  
Batten Disease ◽  
Storage Material ◽  
Subunit C ◽  
Mitochondrial Atp Synthase

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 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.

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