NDLI: The F1F0-ATP synthase complex influences the assembly state of the cytochrome bc1-cytochrome oxidase supercomplex and its association with the TIM23 machinery.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Dienhart, Mary K. Saddar, Sonika Stuart, Rosemary A.
Description	Author Affiliation: Saddar S ( Department of Biological Sciences, Marquette University, Milwaukee, Wisconsin 53233, USA.)
Abstract	The enzyme complexes involved in mitochondrial oxidative phosphorylation are organized into higher ordered assemblies termed supercomplexes. Subunits e and g (Su e and Su g, respectively) are catalytically nonessential subunits of the F1F0-ATP synthase whose presence is required to directly support the stable dimerization of the ATP synthase complex. We report here that Su g and Su e are also important for securing the correct organizational state of the cytochrome bc1-cytochrome oxidase (COX) supercomplex. Mitochondria isolated from the Delta su e and Delta su g null mutant strains exhibit decreased levels of COX enzyme activity but appear to have normal COX subunit protein levels. An altered stoichiometry of the cytochrome bc1-COX supercomplex was observed in mitochondria deficient in Su e and/or Su g, and a perturbation in the association of Cox4, a catalytically important subunit of the COX complex, was also detected. In addition, an increase in the level of the TIM23 translocase associated with the cytochrome bc1-COX supercomplex is observed in the absence of Su e and Su g. Together, our data highlight that a further level of complexity exists between the oxidative phosphorylation supercomplexes, whereby the organizational state of one complex, i.e. the ATP synthase, may influence that of another supercomplex, namely the cytochrome bc1-COX complex.
ISSN	00219258
e-ISSN	1083351X
Journal	Journal of Biological Chemistry
Issue Number	11
Volume Number	283
Language	English
Publisher	American Society for Biochemistry and Molecular Biology (United States)
Publisher Date	2008-03-14
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Electron Transport Complex III Chemistry Electron Transport Complex IV Membrane Transport Proteins Mitochondrial Proton-Translocating ATPases Metabolism Saccharomyces Cerevisiae Proteins Saccharomyces Cerevisiae Enzymology Chromatography, Gel Dimerization Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Mitochondria Models, Biological Oxygen Phosphorylation Protein Structure, Tertiary Research Support, N.I.H., Extramural Biochemistry Molecular Biology
Content Type	Text
Resource Type	Article
Subject	Cell Biology Biochemistry Molecular Biology

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