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Molecular determinants of dihydrouridine synthase activity
Author(s) -
Savage Dan F.,
de Crécy-Lagard Valérie,
Bishop Anthony C.
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2006.08.062
Subject(s) - aquifex aeolicus , complementation , biochemistry , atp synthase , escherichia coli , enzyme , biology , transfer rna , chemistry , gene , microbiology and biotechnology , rna , phenotype
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.