2-Thiouridine formation in : a critical review.

Modifications of transfer RNA (tRNA) have been shown to play critical roles in the biogenesis, metabolism, structural stability, and function of RNA molecules, and the specific modifications of nucleobases with sulfur atoms in tRNA are present in prokaryotes and eukaryotes. The s group of sU34 stabilizes anticodon structure, confers ribosome-binding ability to tRNA, and improves reading frame maintenance. In particular, specific enzymes catalyze the biosynthesis of sulfur-containing nucleosides of sU34, such as the L-cysteine desulfurase IscS and the tRNA thiouridylase MnmA in . Until recently, the mechanism of sulfur transfer in was considered to involve persulfide chemistry; however, a newly proposed mechanism suggests the involvement of a [4Fe-4S] cluster bound to MnmA. This review provides a critical appraisal of recent evidence for [4Fe-4S]-dependent or [4Fe-4S]-independent tRNA thiolation in 2-thiouridine formation.