期刊
FEBS LETTERS
卷 580, 期 22, 页码 5198-5202出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.febslet.2006.08.062
关键词
tRNA; tRNA modification; dihydrouridine; dihydrouridine synthase; YjbN; site-directed mutagenesis
资金
- NCRR NIH HHS [P41 RR-01081] Funding Source: Medline
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. (c) 2006 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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