"Molecular determinants of dihydrouridine synthase activity."
Savage DF, de Crecy-Lagard V, Bishop AC
Published 2006-10-02 in FEBS Lett volume 580 .
Pubmed ID: 16962594
DOI identifier: -
|Dihydrouridine is one of the most abundant modified bases in tRNA. However, little is known concerning the biochemistry of dihydrouridine synthase (DUS) enzymes. To identify molecular determinants that are necessary for DUS activity, we have developed a DUS-complementation assay in Escherichia coli. Using this assay, we have identified amino-acid residues that are critical for the activity of YjbN, an E. coli DUS. We also show that the aq1598 gene product, a putative DUS from Aquifex aeolicus, catalyzes dihydrouridine formation, providing the first biochemical demonstration that A. aeolicus encodes an active DUS.|
This publication refers to following proteins:
- DusA (Escherichia coli)
- DusB (Escherichia coli)
- DusC (Escherichia coli)
Last modification of this entry: Sept. 6, 2012