Affiliation:
1. Department of Cell Biology, Biozentrum, University of Basel, 4056 Basel, Switzerland.
Abstract
Several transfer RNAs (tRNAs) contain inosine (I) at the first position of their anticodon (position 34); this modification is thought to enlarge the codon recognition capacity during protein synthesis. The tRNA-specific adenosine deaminase of
Saccharomyces cerevisiae
that forms I
34
in tRNAs is described. The heterodimeric enzyme consists of two sequence-related subunits (Tad2p/ADAT2 and Tad3p/ADAT3), both of which contain cytidine deaminase (CDA) motifs. Each subunit is encoded by an essential gene (
TAD2
and
TAD3
), indicating that I
34
is an indispensable base modification in elongating tRNAs. These results provide an evolutionary link between the CDA superfamily and RNA-dependent adenosine deaminases (ADARs/ADATs).
Publisher
American Association for the Advancement of Science (AAAS)
Cited by
281 articles.
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