A tRNA circularization assay: Evidence for the variation of the conformation of the CCA end

• Published in: RNA (Cambridge) Vol. 4; no. 7; pp. 733 - 738
• Main Authors: HOU, YA-MING, LIPMAN, RICHARD S.A., ZARUTSKIE, JENNIFER A.
• Format: Journal Article
• Language: English
• Published: United States Cambridge University Press 01.07.1998
• Subjects: Amino Acyl-tRNA Synthetases - metabolism; Base Sequence; Binding Sites; Escherichia coli; Letter; LETTER TO THE EDITOR; Molecular Sequence Data; Nucleic Acid Conformation; Polynucleotide Ligases - metabolism; RNA, Bacterial - chemistry; RNA, Transfer, Cys - chemistry; Virus Replication; replication; tRNA circularization; aminoacylation; E. coli tRNACys; T4 RNA ligase
• ISSN: 1355-8382; 1469-9001
• DOI: 10.1017/S1355838298980281

The CCA end is common to all tRNAs as the universal site for amino acid attachment. It is also conserved in the 3′-terminal tRNA-like structure of viral genomes that can be aminoacylated by an aminoacyl-tRNA synthetase (Florentz & Giegé, 1995). During aminoacylation, the CCA end enters the catalytic center of an aminoacyl-tRNA synthetase and provides the site for chemistry to take place. The CCA end is also widely used in replication of retroviruses, the bacterial single-stranded RNA viruses, and duplex DNA plasmids of fungal mitochondria. During replication, the CCA end interacts with the template-specificity domain of reverse transcriptase or replicase and provides the initiation site for primer binding and extension (Maizels & Weiner, 1994). The importance of the CCA end in translation and in replication suggests that its conformation will play a role in these two fundamental processes.