Abstract
Selenophosphate synthetase (SelD) generates the selenium donor for selenocysteine tRNA biosynthesis in E. coli. One homolog of SelD in eukaryotes is selenophosphate synthetase 1 (SPS1). A second selenophosphate synthetase (SPS2) was also previously identified and it is a selenoprotein in mammals. Knockdown of SPS2 in NIH3T3 cells using RNAi technology showed that selenoprotein biosynthesis was severely impaired, while knockdown of SPS1 had no effect. In vitro, ATP hydrolysis to AMP in the presence of selenium was much more efficient with SPS2 than E. coli SelD, while such activity of mouse SPS1 was not dependent on selenium. These studies indicated that SPS2 provides the active selenium donor for selenocysteine biosynthesis in mammals and SPS1 has a separate function in Sec biosynthesis. This research was supported by the Intramural Research Program of the NIH, NCI, CCR, and by NIH GM061603.
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