22 research outputs found
Identification of the methyltransferase targeting C2499 in Deinococcus radiodurans 23S ribosomal RNA
Problems and Prospects in the Characterization of Posttranscriptional Modifications in Large RNAs
Stable Isotope Labeling for Improved Comparative Analysis of RNA Digests by Mass Spectrometry
Biochemical and Computational Analysis of the Substrate Specificities of Cfr and RlmN Methyltransferases
The effect of mesoporous support on the catalytic performance of Pd nanoparticles in the hydrogenation of cyclopentene
Common thiolation mechanism in the biosynthesis of tRNA thiouridine and sulphur-containing cofactors
2-Thioribothymidine (s2T), a modified uridine, is found at position 54 in transfer RNAs (tRNAs) from several thermophiles; s2T stabilizes the L-shaped structure of tRNA and is essential for growth at higher temperatures. Here, we identified an ATPase (tRNA-two-thiouridine C, TtuC) required for the 2-thiolation of s2T in Thermus thermophilus and examined in vitro s2T formation by TtuC and previously identified s2T-biosynthetic proteins (TtuA, TtuB, and cysteine desulphurases). The C-terminal glycine of TtuB is first activated as an acyl-adenylate by TtuC and then thiocarboxylated by cysteine desulphurases. The sulphur atom of thiocarboxylated TtuB is transferred to tRNA by TtuA. In a ttuC mutant of T. thermophilus, not only s2T, but also molybdenum cofactor and thiamin were not synthesized, suggesting that TtuC is shared among these biosynthetic pathways. Furthermore, we found that a TtuB–TtuC thioester was formed in vitro, which was similar to the ubiquitin-E1 thioester, a key intermediate in the ubiquitin system. The results are discussed in relation to the mechanism and evolution of the eukaryotic ubiquitin system