TY  - JOUR
A1  - Chowdhury, Mita Mullick
A1  - Dosche, Carsten
A1  - Loehmannsröben, Hans-Gerd
A1  - Leimkühler, Silke
T1  - Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans
T2  - The journal of biological chemistry
N2  - We studied two pathways that involve the transfer of persulfide sulfur in humans, molybdenum cofactor biosynthesis and tRNA thiolation. Investigations using human cells showed that the two-domain protein MOCS3 is shared between both pathways. MOCS3 has an N-terminal adenylation domain and a C-terminal rhodanese-like domain. We showed that MOCS3 activates both MOCS2A and URM1 by adenylation and a subsequent sulfur transfer step for the formation of the thiocarboxylate group at the C terminus of each protein. MOCS2A and URM1 are beta-grasp fold proteins that contain a highly conserved C-terminal double glycine motif. The role of the terminal glycine of MOCS2A and URM1 was examined for the interaction and the cellular localization with MOCS3. Deletion of the C-terminal glycine of either MOCS2A or URM1 resulted in a loss of interaction with MOCS3. Enhanced cyan fluorescent protein and enhanced yellow fluorescent protein fusions of the proteins were constructed, and the fluorescence resonance energy transfer efficiency was determined by the decrease in the donor lifetime. The cellular localization results showed that extension of the C terminus with an additional glycine of MOCS2A and URM1 altered the localization of MOCS3 from the cytosol to the nucleus.
Y1  - 2012
UR  - https://publishup.uni-potsdam.de/frontdoor/index/index/docId/35897
SN  - 0021-9258
VL  - 287
IS  - 21
SP  - 17297
EP  - 17307
PB  - American Society for Biochemistry and Molecular Biology
CY  - Bethesda
ER  -