The effect of point mutations affecting Escherichia coli tryptophan tRNA on anticodon-anticodon interactions and on UGA suppression

Vacher, Jean; Grosjean, Henri; Houssier, Claude; Buckingham, Richard H.

doi:10.1016/0022-2836(84)90460-1

Cited by 68 publications

(42 citation statements)

References 25 publications

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“…Other observations, using cell-free protein synthesis systems, stressed that the rate of translation of a given mRNA was optimal in the presence of tRNA from the homologous tissue (Le Meur et al 1976;Sharma and Beezley 1976). It is worth mentioning early works emphasizing the biological importance of posttranscriptional modifications of tRNA (Björk and Neidhardt 1975;Ny and Björk 1977;Labuda et al 1982;Vacher et al 1984;Meier et al 1985;Grosjean et al 1995).…”

Section: The State Of the Trna Population In The Cellmentioning

confidence: 99%

Protein folding and tRNA biology

2017

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Polypeptides can fold into tertiary structures while they are synthesized by the ribosome. In addition to the amino acid sequence, protein folding is determined by several factors within the cell. Among others, the folding pathway of a nascent polypeptide can be affected by transient interactions with other proteins, ligands, or the ribosome, as well as by the translocation through membrane pores. Particularly, the translation machinery and the population of tRNA under different physiological or adaptive responses can dramatically affect protein folding. This review summarizes the scientific evidence describing the role of translation kinetics and tRNA populations on protein folding and addresses current efforts to better understand tRNA biology. It is organized into three main parts, which are focused on: (i) protein folding in the cellular context; (ii) tRNA biology and the complexity of the tRNA population; and (iii) available methods and technical challenges in the characterization of tRNA pools. In this manner, this work illustrates the ways by which functional properties of proteins may be modulated by cellular tRNA populations.

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Section: The State Of the Trna Population In The Cellmentioning

confidence: 99%

Protein folding and tRNA biology

2017

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“…The greatest diversity of tRNA modifications occurs on nucleotides 34 and 37 in the anticodon loop (ACL), which optimize codon:anticodon fit in the ribosome and promote translational fidelity (Gefter 1969;Vacher et al 1984;Ericson and Bjork 1991;Jenner et al 2010). Here we examine yeasts' tRNA isopentenyltransferases (i.e., dimethylallyltransferase, DMATase, members of the D 2 -isopentenylpyrophosphate transferase, IPPT superfamily) encoded by tit1 + in Schizosaccharomyces pombe and MOD5 in Saccharomyces cerevisiae, whose functional homologs are Escherichia coli miaA, human tumor suppressor TRIT1, and the Caenorhabditis elegans life-span gene product GRO-1, which convert A37 to N 6 -(isopentenyl)adenosine (i 6 A37) in their target tRNAs (Dihanich et al 1987;Soderberg and Poulter 2000;Lemieux et al 2001;Spinola et al 2005).…”

Section: Introductionmentioning

confidence: 99%

Plasticity and diversity of tRNA anticodon determinants of substrate recognition by eukaryotic A37 isopentenyltransferases

Lamichhane¹,

Blewett²,

Maraia³

2011

RNA

137

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The N 6 -(isopentenyl)adenosine (i 6 A) modification of some tRNAs at position A37 is found in all kingdoms and facilitates codonspecific mRNA decoding, but occurs in different subsets of tRNAs in different species. Here we examine yeasts' tRNA isopentenyltransferases (i.e., dimethylallyltransferase, DMATase, members of the D 2 -isopentenylpyrophosphate transferase, IPPT superfamily) encoded by tit1 + in Schizosaccharomyces pombe and MOD5 in Saccharomyces cerevisiae, whose homologs are Escherichia coli miaA, the human tumor suppressor TRIT1, and the Caenorhabditis elegans life-span gene product GRO-1. A major determinant of miaA activity is known to be the single-stranded tRNA sequence, A36A37A38, in a stem-loop. tRNA Trp CCA from either yeast is a Tit1p substrate, but neither is a Mod5p substrate despite the presence of A36A37A38. We show that Tit1p accommodates a broader range of substrates than Mod5p. tRNA Trp CCA is distinct from Mod5p substrates, which we sort into two classes based on the presence of G at position 34 and other elements. A single substitution of C34 to G converts tRNA Trp CCA to a Mod5p substrate in vitro and in vivo, consistent with amino acid contacts to G34 in existing Mod5p-tRNA Cys GCA crystal structures. Mutation of Mod5p in its G34 recognition loop region debilitates it differentially for its G34 (class I) substrates. Multiple alignments reveal that the G34 recognition loop sequence of Mod5p differs significantly from Tit1p, which more resembles human TRIT1 and other DMATases. We show that TRIT1 can also modify tRNA Trp CCA consistent with broad recognition similar to Tit1p. This study illustrates previously unappreciated molecular plasticity and biological diversity of the tRNA-isopentenyltransferase system of eukaryotes.

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“…3, 4, and 9). The ms 2 i 6 A37 tRNA modification is thought to stabilize tRNA-mRNA interactions by improving intrastrand stacking within tRNA anticodon loops and interstrand stacking between codons and anticodons (10,11). ms 2 i 6 A37 also seems to influence the conformation of the tRNA anticodon loop and thereby affect interstrand stacking interactions between wobble bases at position 34 in tRNA and bases immediately 3Ј to codons (4,10).…”

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confidence: 99%