TRNA-dihydrouridine synthase

Last updated
Dihydrouridine synthase (Dus)
PDB 1vhn EBI.jpg
crystal structure of a putative flavin oxidoreductase with flavin
Identifiers
SymbolDus
Pfam PF01207
Pfam clan CL0036
InterPro IPR001269
PROSITE PDOC00874
SCOP2 1vhn / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

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

  1. 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.
  2. 1 2 Xing F, Martzen MR, Phizicky EM (March 2002). "A conserved family of Saccharomyces cerevisiae synthases effects dihydrouridine modification of tRNA". RNA. 8 (3) S1355838202029825: 370–81. doi:10.1017/S1355838202029825. PMC   1370258 . PMID   12003496.
This article incorporates text from the public domain Pfam and InterPro: IPR001269