Glycine Codon Discrimination and the Nucleotide inPosition 32 of the Anticodon Loop

Claesson, Catharina; Lustig, Florentyna; Borén, Thomas; Simonsson, Carolina; Barciszewska, Mirosława Z.; Lagerkvist, Ulf

doi:10.1006/jmbi.1994.0132

Cited by 37 publications

(32 citation statements)

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“…Subsequent in vivo studies of the translation efficiency of E. coli suppressor tRNAs (Yarus et al 1986;Kleina et al 1990;Yarus and Smith 1995) and in vitro biochemical studies of tRNA binding to the ribosome decoding center (A site) (Lustig et al 1993;Claesson et al 1995;Konevega et al 2004;Olejniczak et al 2005) have chiefly focused on the residues of the anticodon loop. When taken together, the results of these studies show that the residue at position 37, which is adjacent to the third anticodon nucleotide, and the residues of the [32][33][34][35][36][37][38] pseudopair, at the top of the anticodon loop, can affect translation efficiency and binding to the cognate codon.…”

Section: Discussionmentioning

confidence: 99%

Anticodon-dependent conservation of bacterial tRNA gene sequences

Saks

Conery²

2007

RNA

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The residues in tRNA that account for its tertiary fold and for its specific aminoacylation are well understood. In contrast, relatively little is known about the residues in tRNA that dictate its ability to transit the different sites of the ribosome. Yet protein synthesis cannot occur unless tRNA properly engages with the ribosome. This study analyzes tRNA gene sequences from 145 fully sequenced bacterial genomes. Grouping the sequences according to the anticodon triplet reveals that many residues in tRNA, including some that are distal to the anticodon loop, are conserved in an anticodon-dependent manner. These residues evade detection when tRNA genes are grouped according to amino acid family. The conserved residues include those at positions 32, 38, and 37 of the anticodon loop, which are already known to influence tRNA translational performance. Therefore, it seems likely that the newly detected anticodon-associated residues also influence tRNA performance on the ribosome. Remarkably, tRNA genes that belong to the same amino acid family and therefore share identical residues at the second and third anticodon positions have diverged, during bacterial evolution, into highly conserved groups that are defined by the residue at the first (wobble) anticodon position. Current ideas about the properties of tRNA and the translation mechanism do not fully account for this phenomenon. The results of the present study provide a foundation for studying the adaptation of individual tRNAs to the translation machinery and for future studies of the translation mechanism.

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Section: Discussionmentioning

confidence: 99%

Anticodon-dependent conservation of bacterial tRNA gene sequences

Saks

Conery²

2007

RNA

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“…Many experimental data suggest that some nucleotides outside the anticodon may influence the decoding activity of the tRNA molecule (Agris, 2004;Claesson et al, 1995;Curran, 1998;Hirsh, 1971;Li et al, 1997;Lustig et al, 1993;Yarian et al, 2000;Yarus, 1982;Yarus et al, 1986). Some of these effects may be specific for some limited codons.…”

Section: Discrimination Of Two Different Aminoacyl-trna Speciesmentioning

confidence: 94%

Classification of the possible pairs between the first anticodon and the third codon positions based on a simple model assuming two geometries with which the pairing effectively potentiates the decoding complex

Takai

2006

Journal of Theoretical Biology

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“…In wild type M. mycoides tRNA Gly , the anticodon UCC failed to discriminate between the glycine codons with a position 32 cytidine, but when changed to a U it acted like E. coli tRNAs and discriminated between the four glycine codons. 62 In M. mycoides , the single tRNA Gly UCC that decodes all four glycine codons is devoid of anticodon modifications and has a C 32 ○A 38 mismatch which leads to decreased fidelity in vivo (Fig. 4).…”

Section: Unmodified Wobble Position 34 and The Importance Of Position 32mentioning

confidence: 99%

“…Thus, the nature of the N 32 ○N 38 base interaction affects the binding of the anticodon to the codon suggesting that the intraloop hydrogen bonding alters the conformation and dynamics of the anticodon stem and loop domain within the ribosomal complex. 62,70 …”

Section: Unmodified Wobble Position 34 and The Importance Of Position 32mentioning

confidence: 99%

Celebrating wobble decoding: Half a century and still much is new

et al. 2017

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A simple post-transcriptional modification of tRNA, deamination of adenosine to inosine at the first, or wobble, position of the anticodon, inspired Francis Crick's Wobble Hypothesis 50 years ago. Many more naturally-occurring modifications have been elucidated and continue to be discovered. The post-transcriptional modifications of tRNA's anticodon domain are the most diverse and chemically complex of any RNA modifications. Their contribution with regards to chemistry, structure and dynamics reveal individual and combined effects on tRNA function in recognition of cognate and wobble codons. As forecast by the Modified Wobble Hypothesis 25 years ago, some individual modifications at tRNA's wobble position have evolved to restrict codon recognition whereas others expand the tRNA's ability to read as many as four synonymous codons. Here, we review tRNA wobble codon recognition using specific examples of simple and complex modification chemistries that alter tRNA function. Understanding natural modifications has inspired evolutionary insights and possible innovation in protein synthesis.

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Glycine Codon Discrimination and the Nucleotide inPosition 32 of the Anticodon Loop

Cited by 37 publications

References 0 publications

Anticodon-dependent conservation of bacterial tRNA gene sequences

Anticodon-dependent conservation of bacterial tRNA gene sequences

Classification of the possible pairs between the first anticodon and the third codon positions based on a simple model assuming two geometries with which the pairing effectively potentiates the decoding complex

Celebrating wobble decoding: Half a century and still much is new

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