English (United Kingdom)

https://curated-unify.zendy.io/wp-json/zendy-region/v1/featured_content/oa?rat=en

https://curated-unify.zendy.io/wp-json/zendy-region/v1/highlighted_journal/

Zendy Pro

Presents the zaia usage as premium feature

ZAIA

Presents AI Discovery search usage as a premium feature

AI Discovery

Presents AI Discovery explain and summary usage as a premium feature

Content Analysis

Presents the keyphrase highlighting as premium feature

Keyphrase Highlighting

Presents the summarisation as premium feature

Summarisation

Presents the pdf analysis as premium feature

PDF Analysis

1500 Top-up

3000 Top-up

Zendy Basic

2500 Top-up

Zendy Unlimited

Presents the access of premium content as premium feature

Premium Content

The CCA end is common to all tRNAs as the universal site for amino acid attachment+ It is also conserved in the 39-terminal tRNA-like structure of viral genomes that can be aminoacylated by an aminoacyl-tRNA synthetase (Florentz & Giege, 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 singlestranded 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+ Previous studies indicate that the N73 nucleotide and aC 1 :A72 mismatch have the ability to manipulate the conformation of the CCA end+ An NMR analysis of tRNA acceptor stems (Puglisi et al+, 1994) showed that the CCA end preceded by an A73 nucleotide has an extended conformation, whereas that preceded by a U73 has a fold-back structure+ The fold-back structure of the CCA end brings the terminal A76 adjacent to the 59 side of the acceptor stem and may be stabilized by a weak hydrogen bond between A76 and U73+ The folded CCA end is also found in the crystal structure of the Escherichia coli initiator tRNA fMet which, despite having an A73, carries an unusual C1:A72 mismatch that is thought to contribute to the fold-back of the CCA end (Schevitz et al+, 1979; Woo et al+, 1980; Ferguson & Yang, 1986; Pscheidt & Wells, 1986)+ In tRNA fMet ,

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