Abstract
The abundance in vivo of each of three subunits b, OSCP and d, components of the stalk region of the yeast mitochondrial ATP synthase complex, was manipulated by a controlled depletion strategy. Western blots of whole cell lysates were used to study the effect of depletion of each of these subunits on the cellular levels of other subunits of the enzyme complex. A hierarchy of subunit stability was determined and interpreted to indicate the order of assembly of these three subunits of the stalk region. Thus, subunit b is assembled first, followed by OSCP and then by subunit d.
Copyright 1998 Elsevier Science B.V. All rights reserved.
Publication types
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Adenosine Triphosphatases / genetics
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Adenosine Triphosphatases / metabolism*
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Carrier Proteins*
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Immunoblotting
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Intracellular Membranes / enzymology
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Membrane Proteins / genetics
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Membrane Proteins / metabolism
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Mitochondria / enzymology*
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Mitochondrial Proton-Translocating ATPases
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Proteins / genetics
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Proteins / metabolism
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Proton-Translocating ATPases / genetics
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Proton-Translocating ATPases / metabolism
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Saccharomyces cerevisiae / enzymology*
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Saccharomyces cerevisiae / genetics
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Saccharomyces cerevisiae Proteins*
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Vacuolar Proton-Translocating ATPases*
Substances
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Carrier Proteins
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Membrane Proteins
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Proteins
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Saccharomyces cerevisiae Proteins
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VMA8 protein, S cerevisiae
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Adenosine Triphosphatases
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Vacuolar Proton-Translocating ATPases
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Mitochondrial Proton-Translocating ATPases
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Proton-Translocating ATPases
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oligomycin sensitivity-conferring protein