tRNA-dihydrouridine synthase
| Dihydrouridine synthase (Dus) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of a putative flavin oxidoreductase with flavin | |||||||||
| Identifiers | |||||||||
| Symbol | Dus | ||||||||
| Pfam | PF01207 | ||||||||
| Pfam clan | CL0036 | ||||||||
| InterPro | IPR001269 | ||||||||
| PROSITE | PDOC00874 | ||||||||
| SCOP2 | 1vhn / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, tRNA-dihydrouridine synthase is a family of enzymes which catalyse the reduction of the 5,6-double bond of a uridine residue on tRNA. Dihydrouridine modification of tRNA is widely observed in prokaryotes and eukaryotes, and also in some archaea. Most dihydrouridines are found in the D loop of t-RNAs. The role of dihydrouridine in tRNA is currently unknown, but may increase conformational flexibility of the tRNA. It is likely that different family members have different substrate specificities, which may overlap. Dus 1 from Saccharomyces cerevisiae (Baker's yeast) acts on pre-tRNA-Phe, while Dus 2 acts on pre-tRNA-Tyr and pre-tRNA-Leu. Dus 1 is active as a single subunit, requiring NADPH or NADH, and is stimulated by the presence of FAD.[1][2] Some family members may be targeted to the mitochondria and even have a role in mitochondria.[2]
References[edit]
- ^ Xing, F.; Hiley, S. L.; Hughes, T. R.; Phizicky, E. M. (2004). "The Specificities of Four Yeast Dihydrouridine Synthases for Cytoplasmic tRNAs". Journal of Biological Chemistry. 279 (17): 17850–17860. doi:10.1074/jbc.M401221200. PMID 14970222.
- ^ a b Xing F, Martzen MR, Phizicky EM (March 2002). "A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA". RNA. 8 (3): 370–81. doi:10.1017/S1355838202029825. PMC 1370258. PMID 12003496.