TY  - JOUR
A1  - Marelja, Zvonimir
A1  - Chowdhury, Mita Mullick
A1  - Dosche, Carsten
A1  - Hille, Carsten
A1  - Baumann, Otto
A1  - Löhmannsröben, Hans-Gerd
A1  - Leimkühler, Silke
T1  - The L-cysteine desulfurase NFS1 is localized in the cytosol where it provides the sulfur for molybdenum cofactor biosynthesis in humans
T2  - PLoS one
N2  - In humans, the L-cysteine desulfurase NFS1 plays a crucial role in the mitochondrial iron-sulfur cluster biosynthesis and in the thiomodification of mitochondrial and cytosolic tRNAs. We have previously demonstrated that purified NFS1 is able to transfer sulfur to the C-terminal domain of MOCS3, a cytosolic protein involved in molybdenum cofactor biosynthesis and tRNA thiolation. However, no direct evidence existed so far for the interaction of NFS1 and MOCS3 in the cytosol of human cells. Here, we present direct data to show the interaction of NFS1 and MOCS3 in the cytosol of human cells using Forster resonance energy transfer and a split-EGFP system. The colocalization of NFS1 and MOCS3 in the cytosol was confirmed by immunodetection of fractionated cells and localization studies using confocal fluorescence microscopy. Purified NFS1 was used to reconstitute the lacking molybdoenzyme activity of the Neurospora crassa nit-1 mutant, giving additional evidence that NFS1 is the sulfur donor for Moco biosynthesis in eukaryotes in general.
Y1  - 2013
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/35083
SN  - 1932-6203
VL  - 8
IS  - 4
PB  - PLoS
CY  - San Fransisco
ER  -