Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans.

@article{Chowdhury2012DualRO,
  title={Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans.},
  author={Mita Mullick Chowdhury and Carsten Dosche and Hans-Gerd L{\"o}hmannsr{\"o}ben and Silke Leimk{\"u}hler},
  journal={The Journal of biological chemistry},
  year={2012},
  volume={287 21},
  pages={
          17297-307
        }
}
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… CONTINUE READING

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