Antibodies against subunits of F0 sector of ATP synthase from Saccharomyces cerevisiae. Stimulation of ATP synthase by subunit-8-reactive antibodies and inhibition by subunit-9-reactive antibodies
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چکیده
منابع مشابه
Entrapment of water by subunit c of ATP synthase
We consider an ancient protein, and water as a smooth surface, and show that the interaction of the two allows the protein to change its hydrogen bonding to encapsulate the water. This property could have made a three-dimensional microenvironment, 3-4 Gyr ago, for the evolution of subsequent complex water-based chemistry. Proteolipid, subunit c of ATP synthase, when presented with a water surfa...
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Ian M. FEARNLEY,* John E. WALKER,*§ Ryan D. MARTINUS,t Robert D. JOLLY,t K. Brett KIRKLAND,t G. John SHAWI and David N. PALMERt * M.R.C. Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, U.K., t Department of Veterinary Pathology and Public Health, Massey University, Palmerston North, New Zealand, and t Biotechnology Division, Department of Scientific and Industrial Research, Palm...
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The F1Fo-ATP synthases of alkaliphilic bacteria exhibit latent ATPase activity, and for the thermoalkaliphile Bacillus sp. strain TA2.A1, this activity is intrinsic to the F1 moiety. To study the mechanism of ATPase inhibition, we developed a heterologous expression system in Escherichia coli to produce TA2F1 complexes from this thermoalkaliphile. Like the native F1Fo-ATP synthase, the recombin...
متن کاملImpaired ATP synthase assembly associated with a mutation in the human ATP synthase subunit 6 gene.
Mutations in human mitochondrial DNA are a well recognized cause of disease. A mutation at nucleotide position 8993 of human mitochondrial DNA, located within the gene for ATP synthase subunit 6, is associated with the neurological muscle weakness, ataxia, and retinitis pigmentosa (NARP) syndrome. To enable analysis of this mutation in control nuclear backgrounds, two different cell lines were ...
متن کاملCrystallization of the catalytic subunit of Saccharomyces cerevisiae acetohydroxyacid synthase.
Acetohydroxyacid synthase (AHAS; E.C. 4.1.3.18) is the first enzyme in the biosynthetic pathway of the branched-chain amino acids isoleucine, leucine and valine. It is a thiamin diphosphate-dependent enzyme which catalyses the decarboxylation of pyruvate and its condensation with either 2-ketobutyrate or a second molecule of pyruvate to give 2-aceto-2-hydroxybutyrate or 2-acetolactate, respecti...
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ژورنال
عنوان ژورنال: European Journal of Biochemistry
سال: 1994
ISSN: 0014-2956,1432-1033
DOI: 10.1111/j.1432-1033.1994.tb19021.x