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Functional sulfurtransferase is associated with mitochondrial complex I from Yarrowia lipolytica, but is not required for assembly of its iron-sulfur clusters
Authors:Abdrakhmanova Albina  Dobrynin Krzysztof  Zwicker Klaus  Kerscher Stefan  Brandt Ulrich
Institution:Ulrich Brandt, Universit?t Frankfurt, Fachbereich Medizin, Zentrum der Biologischen Chemie, Molekulare Bioenergetik, Theodor-Stern-Kai 7, Haus 26, 60590 Frankfurt am Main, Germany.
Abstract:Here, we report that in the obligate aerobic yeast Yarrowia lipolytica, a protein exhibiting rhodanese (thiosulfate:cyanide sulfurtransferase) activity is associated with proton pumping NADH:ubiquinone oxidoreductase (complex I). Complex I is a key enzyme of the mitochondrial respiratory chain that contains eight iron-sulfur clusters. From a rhodanese deletion strain, we purified functional complex I that lacked the additional protein but was fully assembled and displayed no functional defects or changes in EPR signature. In contrast to previous suggestions, this indicated that the sulfurtransferase associated with Y. lipolytica complex I is not required for assembly of its iron-sulfur clusters.
Keywords:BN-PAGE  blue-native polyacrylamide gel electrophoresis  DBQ  n-decylubiquinone  dNADH  deamino-nicotinamide-adenine-dinucleotide (reduced form)  dSDS-PAGE  doubled sodium dodecylsulfate-polyacrylamide gel electrophoresis  HAR  hexa-ammine-ruthenium(III)-chloride  MALDI-TOF MS  matrix-assisted laser desorption/ionisation-time of flight mass spectrometry  MST  3-mercaptopyruvate sulfurtransferase  TST  thiosulfate sulfurtransferase
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