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Dihydrouridine synthase catalyzes reduction of the 5,6-double bond of a uridine residue on the displacement loop of tRNA.
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Here, the X-ray crystal structure of a construct of hDus2 encompassing the catalytic and tRNA-recognition domains (residues 1-340) determined at 1.9 A resolution is presented.
hDUS2 interacts with protein kinase (show CDK7 Antibodies) PKR (show PKLR Antibodies) through its dsRNA binding/dimerization domain and inhibits its kinase activity.
This gene encodes a cytoplasmic protein that catalyzes the conversion of uridine residues to dihydrouridine in the D-loop of tRNA. The resulting modified bases confer enhanced regional flexibility to tRNA. The encoded protein may increase the rate of translation by inhibiting an interferon-induced protein kinase. This gene has been implicated in pulmonary carcinogenesis. Alternatively spliced transcript variants have been described for this gene.
tRNA-dihydrouridine synthase 2-like
, dihydrouridine synthase 2-like, SMM1 homolog (S. cerevisiae)
, dihydrouridine synthase 2-like, SMM1 homolog
, SMM1 homolog
, tRNA-dihydrouridine(20) synthase [NAD(P)+]-like
, up-regulated in lung cancer protein 8