TY  - JOUR
A1  - Burschel, Sabrina
A1  - Decovic, Doris Kreuzer
A1  - Nuber, Franziska
A1  - Stiller, Marie
A1  - Hofmann, Maud
A1  - Zupok, Arkadiusz
A1  - Siemiatkowska, Beata
A1  - Gorka, Michal Jakub
A1  - Leimkühler, Silke
A1  - Friedrich, Thorsten
T1  - Iron-sulfur cluster carrier proteins involved in the assembly of Escherichia coli NADH
BT  - ubiquinone oxidoreductase (complex I)
JF  - Molecular microbiology
N2  - The NADH:ubiquinone oxidoreductase (respiratory complex I) is the main entry point for electrons into the Escherichia coli aerobic respiratory chain. With its sophisticated setup of 13 different subunits and 10 cofactors, it is anticipated that various chaperones are needed for its proper maturation. However, very little is known about the assembly of E. coli complex I, especially concerning the incorporation of the iron-sulfur clusters. To identify iron-sulfur cluster carrier proteins possibly involved in the process, we generated knockout strains of NfuA, BolA, YajL, Mrp, GrxD and IbaG that have been reported either to be involved in the maturation of mitochondrial complex I or to exert influence on the clusters of bacterial complex. We determined the NADH and succinate oxidase activities of membranes from the mutant strains to monitor the specificity of the individual mutations for complex I. The deletion of NfuA, BolA and Mrp led to a decreased stability and partially disturbed assembly of the complex as determined by sucrose gradient centrifugation and native PAGE. EPR spectroscopy of cytoplasmic membranes revealed that the BolA deletion results in the loss of the binuclear Fe/S cluster N1b.
Y1  - 2018
U6  - https://doi.org/10.1111/mmi.14137
SN  - 0950-382X
SN  - 1365-2958
VL  - 111
IS  - 1
SP  - 31
EP  - 45
PB  - Wiley
CY  - Hoboken
ER  -