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|Title:||Mutations in mitochondrial complex III uniquely affect complex I in Caenorhabditis elegans|
Phil G. Morgan
Margaret M. Sedensky
Case Western Reserve University
University of Washington, Seattle
|Keywords:||Biochemistry, Genetics and Molecular Biology|
|Citation:||Journal of Biological Chemistry. Vol.285, No.52 (2010), 40724-40731|
|Abstract:||Mitochondrial supercomplexes containing complexes I, III, and IV of the electron transport chain are now regarded as an established entity. Supercomplex I·III·IV has been theorized to improve respiratory chain function by allowing quinone channeling between complexes I and III. Here, we show that the role of the supercomplexes extends beyond channeling. Mutant analysis in Caenorhabditis elegans reveals that complex III affects supercomplex I·III·IV formation by acting as an assembly or stabilizing factor. Also, a complex III mtDNA mutation, ctb-1, inhibits complex I function by weakening the interaction of complex IV in supercomplex I·III·IV. Other complex III mutations inhibit complex I function either by decreasing the amount of complex I (isp-1), or decreasing the amount of complex I in its most active form, the I·III·IV supercomplex (isp-1;ctb-1). ctb-1 suppresses a nuclear encoded complex III defect, isp-1, without improving complex III function. Allosteric interactions involve all three complexes within the supercomplex and are necessary for maximal enzymatic activities. © 2010 by The American Society for Biochemistry and Molecular Biology, Inc.|
|Appears in Collections:||Scopus 2006-2010|
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