INTER-PHYLOGENETIC SPECIFICITY IN THE BONDING OF AMINO ACIDS TO tRNA

Loftfield, Robert B.; Eigner, Elizabeth Ann; Nobel, J. G. De

doi:10.2307/1539625

Cited by 11 publications

(3 citation statements)

References 13 publications

(19 reference statements)

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“…The specific recognition of tRNA by its cognate aminoacyl-tRNA synthetase is determined by identity elements positioned within the tRNA structure. Identity elements have been well-studied after being initially proposed (Loftfield et al 1968) and experimentally verified (Schulman and Pelka 1989;McClain 1993). In the case of arginyl-tRNA synthetase detailed kinetic investigation of yeast transcript variants (Sissler et al 1996) and a study of yeast tRNA mutants conferring lethality in vivo (Geslain et al 2003b) showed that C35 (the 2 nd base of the anticodon) was the major identity element with minor contributions from U/G36.…”

Section: Introductionmentioning

confidence: 99%

The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

Igloi

2021

J Mol Evol

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During the endosymbiotic evolution of mitochondria, the genes for aminoacyl-tRNA synthetases were transferred to the ancestral nucleus. A further reduction of mitochondrial function resulted in mitochondrion-related organisms (MRO) with a loss of the organelle genome. The fate of the now redundant ancestral mitochondrial aminoacyl-tRNA synthetase genes is uncertain. The derived protein sequence for arginyl-tRNA synthetase from thirty mitosomal organisms have been classified as originating from the ancestral nuclear or mitochondrial gene and compared to the identity element at position 20 of the cognate tRNA that distinguishes the two enzyme forms. The evolutionary choice between loss and retention of the ancestral mitochondrial gene for arginyl-tRNA synthetase reflects the coevolution of arginyl-tRNA synthetase and tRNA identity elements.

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Section: Introductionmentioning

confidence: 99%

The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

Igloi

2021

J Mol Evol

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“…It requires a virtually error-free recognition at two levels; the association of one of 20 aminoacyl-tRNA synthetases with its specific amino acid and the simultaneous identification of the cognate tRNA. Heterologous aminoacylation between macromolecules from different species foretold the existence of a common sequence within a given set of tRNAs isoacceptors that is responsible for their specific enzymatic association almost 60 years ago (Loftfield et al 1968 ). However, such tRNA identity elements were experimentally verified only some 20 years later (Normanly et al 1986 ; McClain and Foss 1988 ; Sampson et al 1989 ; Schulman and Pelka 1989 ; Normanly and Abelson 1989 ).…”

Section: Introductionmentioning

confidence: 99%

Evolutionary Adjustment of tRNA Identity Rules in Bacillariophyta for Recognition by an Aminoacyl-tRNA Synthetase Adds a Facet to the Origin of Diatoms

Igloi

2022

J Mol Evol

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Error-free protein synthesis relies on the precise recognition by the aminoacyl-tRNA synthetases of their cognate tRNAs in order to attach the corresponding amino acid. A concept of universal tRNA identity elements requires the aminoacyl-tRNA synthetases provided by the genome of an organism to match the identity elements found in the cognate tRNAs in an evolution-independent manner. Identity elements tend to cluster in the tRNA anticodon and acceptor stem regions. However, in the arginine system, in addition to the anticodon, the importance of nucleotide A20 in the tRNA D-loop for cognate enzyme recognition has been a sustained feature for arginyl-tRNA synthetase in archaea, bacteria and in the nuclear-encoded cytosolic form in mammals and plants. However, nuclear-encoded mitochondrial arginyl-tRNA synthetase, which can be distinguished from its cytosolic form by the presence or absence of signature motifs, dispenses with the A20 requirement. An examination of several hundred non-metazoan organisms and their corresponding tRNAArg substrates has confirmed this general concept to a large extent and over numerous phyla. However, some Stramenopiles, and in particular, Diatoms (Bacillariophyta) present a notable exception. Unusually for non-fungal organisms, the nuclear genome encodes tRNAArg isoacceptors with C or U at position 20. In this case one of two nuclear-encoded cytosolic arginyl-tRNA synthetases has evolved to become insensitive to the nature of the D-loop identity element. The other, with a binding pocket that is compatible with tRNAArg-A20 recognition, is targeted to organelles that encode solely such tRNAs.

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“…Interspecies aminoacylation as a tool for studying the specificity of tRNA aminoacylation was initiated by Benzer and Weissblum [1] in the infancy of aminoacyl-tRNA synthetase research and led to the realization that '... each species of sRNA must have a site or recognition unit which distinguishes it from all other species of sRNA' [2] and 'One must conclude that all tRNA's specific for a particular amino acid contain one or more features in common ...' [3]. After initial chemical approaches to the problem of tRNA recognition [4], the concept of identity was introduced by McClain et al [5], whereas the term 'identity element' was coined by Schulman and Pelka [6].…”

Section: Introductionmentioning

confidence: 99%

The influence of identity elements on the aminoacylation of tRNA^Arg by plant and Escherichia coli arginyl‐tRNA synthetases

2012

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Identity elements determine the accurate recognition between tRNAs and aminoacyl-tRNA synthetases. The arginine system from yeast and Escherichia coli has been studied extensively in the past. However, information about the enzymes from higher eukaryotes is limited and plant aminoacyltRNA synthetases have been largely ignored in this respect. We have designed in vitro tRNA transcripts, based on the soybean tRNA Arg primary structure, aiming to investigate its specific aminoacylation by two recombinant plant arginyl-tRNA synthetases and to compare this with the enzyme from E. coli. Identity elements at positions 20 and 35 in plants parallel those previously established for bacteria. Cryptic identity elements in the plant system that are not revealed within a tRNA Arg consensus sequence compiled from isodecoders corresponding to nine distinct cytoplasmic, mitochondrial and plastid isoaccepting sequences are located in the acceptor stem. Additionally, it has been shown that U20a and A38 are essential for a fully efficient cognate E. coli arginylation, whereas, for the plant arginyl-tRNA synthetases, these bases can be replaced by G20a and C38 with full retention of activity. G10, a constituent of the 10 : 25 : 45 tertiary interaction, is essential for both plant and E. coli activity. Amino acid recognition in terms of discriminating between arginine and canavanine by the arginyl-tRNA synthetase from both kingdoms may be manipulated by changes at different sites within the tRNA structure.

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INTER-PHYLOGENETIC SPECIFICITY IN THE BONDING OF AMINO ACIDS TO tRNA

Cited by 11 publications

References 13 publications

The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

Evolutionary Adjustment of tRNA Identity Rules in Bacillariophyta for Recognition by an Aminoacyl-tRNA Synthetase Adds a Facet to the Origin of Diatoms

The influence of identity elements on the aminoacylation of tRNA^Arg by plant and Escherichia coli arginyl‐tRNA synthetases

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INTER-PHYLOGENETIC SPECIFICITY IN THE BONDING OF AMINO ACIDS TO tRNA

Cited by 11 publications

References 13 publications

The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

The Evolutionary Fate of Mitochondrial Aminoacyl-tRNA Synthetases in Amitochondrial Organisms

Evolutionary Adjustment of tRNA Identity Rules in Bacillariophyta for Recognition by an Aminoacyl-tRNA Synthetase Adds a Facet to the Origin of Diatoms

The influence of identity elements on the aminoacylation of tRNAArg by plant and Escherichia coli arginyl‐tRNA synthetases

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The influence of identity elements on the aminoacylation of tRNA^Arg by plant and Escherichia coli arginyl‐tRNA synthetases