Investigation of a cytosolic sulfur transfer pathway for tRNA thio-modification and biosynthesis of sulfur-containing molecules

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We found that ubiquitin-like protein Urm1 and ubiquitin-activating enzyme-like protein Uba4 were strictly required for the s2 modification. The carboxyl-terminal glycine residue of Urm1 was critical for the s2 modification, indicating direct involvement of the unique ubiquitin-related system in this process. We also demonstrated that the s2 and mcm5 modifications in cytosolic tRNAs influence each other's efficiency. Taken together, our data indicate that the s2 modification of cytosolic tRNAs is a more complex process that requires additional unidentified components.