Volume
579, Issue 30 , 19 December 2005, Pages 6781-6785
doi:10.1016/j.febslet.2005.11.008 
Copyright
© 2005 Federation of European Biochemical Societies Published by Elsevier B.V.
Functional sulfurtransferase is associated with mitochondrial complex I from
Yarrowia lipolytica, but is not required for assembly of its iron–sulfur
clusters
Edited by Peter Brzezinski
Albina Abdrakhmanova, Krzysztof Dobrynin, Klaus Zwicker, Stefan Kerscher and
Ulrich Brandt
, 
Ulrich Brandt, Universität Frankfurt, Fachbereich Medizin,
Zentrum der Biologischen Chemie, Molekulare Bioenergetik, Theodor-Stern-Kai 7,
Haus 26, 60590 Frankfurt am Main, Germany
Received 14 October
2005; revised 2 November 2005; accepted 3 November 2005.
Available online 21 November 2005.
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: Thiosulfate:cyanide sulfurtransferase; Electron
transport complex I; Protein association; Mitochondria
Abbreviations: 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
Corresponding author.
Fax: +49 69 6301 6970.
