Amino acid discrimination by the nuclear encoded mitochondrial arginyl-tRNA synthetase of the larva of a bruchid beetle (Caryedes brasiliensis) from northwestern Costa Rica

Leisinger, Anne-Katrin; Janzen, Daniel H.; Hallwachs, Winnie; Igloi, Gabor L.

doi:10.1016/j.ibmb.2013.10.004

Cited by 11 publications

(6 citation statements)

References 55 publications

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“…In recent years, conflicting evidence has emerged regarding the I34 modification status of tRNA Arg ACG in higher eukaryotes . While I34 could be readily detected by sequencing of tRNA Arg ACG in Escherichia coli , Mycoplasma capricolum , and Saccharomyces cerevisiae , it could not be detected in nematodes, mosses, higher plants, insects, or mammals. − However, the presence of I34 on human tRNA Arg ACG has been documented by other means, suggesting that at least in some of these cases RT-based methods may be leading to artifactual results.…”

Section: Development Of the Methodsmentioning

confidence: 99%

Detection of Inosine on Transfer RNAs without a Reverse Transcription Reaction

et al. 2018

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Inosine at the "wobble" position (I34) is one of the few essential posttranscriptional modifications in tRNAs (tRNAs). It results from the deamination of adenosine and occurs in bacteria on tRNA and in eukarya on six or seven additional tRNA substrates. Because inosine is structurally a guanosine analogue, reverse transcriptases recognize it as a guanosine. Most methods used to examine the presence of inosine rely on this phenomenon and detect the modified base as a change in the DNA sequence that results from the reverse transcription reaction. These methods, however, cannot always be applied to tRNAs because reverse transcription can be compromised by the presence of other posttranscriptional modifications. Here we present SL-ID (splinted ligation-based inosine detection), a reverse transcription-free method for detecting inosine based on an I34-dependent specific cleavage of tRNAs by endonuclease V, followed by a splinted ligation and polyacrylamide gel electrophoresis analysis. We show that the method can detect I34 on different tRNA substrates and can be applied to total RNA derived from different species, cell types, and tissues. Here we apply the method to solve previous controversies regarding the modification status of mammalian tRNA.

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Section: Development Of the Methodsmentioning

confidence: 99%

Detection of Inosine on Transfer RNAs without a Reverse Transcription Reaction

et al. 2018

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“…Extrapolating this observation to the Cyto / Mito system, it is well‐established that the Cyto arginyl‐tRNA synthetase in mammals and plants relies on the presence of A20 . Conversely, Coleopteran Mito tRNA Arg lacks a canonical A20 base and is not aminoacylated by the (Cyto‐like) E. coli enzyme .…”

Section: Resultsmentioning

confidence: 93%

Molecular evidence for the evolution of the eukaryotic mitochondrial arginyl‐tRNA synthetase from the prokaryotic suborder Cystobacterineae

Igloi

2019

FEBS Letters

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The evolutionary origin of the family of eukaryotic aminoacyl‐tRNA synthetases that are essential to all living organisms is a matter of debate. In order to shed molecular light on the ancient source of arginyl‐tRNA synthetase, a total of 1347 eukaryotic arginyl‐tRNA synthetase sequences were mined from databases and analyzed. Their multiple sequence alignment reveals a signature sequence that is characteristic of the nuclear‐encoded enzyme, which is imported into mitochondria. Using this molecular beacon, the origins of this gene can be traced to modern prokaryotes. In this way, a previous phylogenetic analysis linking Myxococcus to the emergence of the eukaryotic mitochondrial arginyl‐tRNA synthetase is supported by the unique existence of the molecular signature within the suborder Cystobacterineae that includes Myxococcus.

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“…23 We have investigated the identity elements that are contained within the structure of the tRNA by systematic base replacements and by transplanting sequence fragments from the cognate tRNA Arg to unrelated mitochondrial tRNAs.…”

Section: Discussionmentioning

confidence: 99%

“…The reaction was initiated by the addition of recombinant C. brasiliensis mitochondrial arginyl-tRNA synthetase 23 to a final concentration of 6 nM. At the given time intervals, 10 ml aliquots were removed and spotted onto 5% TCA-pre-treated Whatman 3 MM discs, washed twice for 10 min with 5% TCA and once with ethanol before air drying and quantification by liquid scintillation counting.…”

Section: Methodsmentioning

confidence: 99%

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Identity elements for the aminoacylation of metazoan mitochondrial tRNA^Arghave been widely conserved throughout evolution and ensure the fidelity of the AGR codon reassignment

Igloi

Leisinger

2014

RNA Biology

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Eumetazoan mitochondrial tRNAs possess structures (identity elements) that require the specific recognition by their cognate nuclear-encoded aminoacyl-tRNA synthetases. The AGA (arginine) codon of the standard genetic code has been reassigned to serine/glycine/termination in eumetazoan organelles and is translated in some organisms by a mitochondrially encoded tRNASerUCU. One mechanism to prevent mistranslation of the AGA codon as arginine would require a set of tRNA identity elements distinct from those possessed by the cytoplasmic tRNAArg in which the major identity elements permit the arginylation of all 5 encoded isoacceptors. We have performed comparative in vitro aminoacylation using an insect mitochondrial arginyl-tRNA synthetase and tRNAArgUCG structural variants. The established identity elements are sufficient to maintain the fidelity of tRNASerUCU reassignment. tRNAs having a UCU anticodon cannot be arginylated but can be converted to arginine acceptance by identity element transplantation. We have examined the evolutionary distribution and functionality of these tRNA elements within metazoan taxa. We conclude that the identity elements that have evolved for the recognition of mitochondrial tRNAArgUCG by the nuclear encoded mitochondrial arginyl-tRNA synthetases of eumetazoans have been extensively, but not universally conserved, throughout this clade. They ensure that the AGR codon reassignment in eumetazoan mitochondria is not compromised by misaminoacylation. In contrast, in other metazoans, such as Porifera, whose mitochondrial translation is dictated by the universal genetic code, recognition of the 2 encoded tRNAArgUCG/UCU isoacceptors is achieved through structural features that resemble those employed by the yeast cytoplasmic system.

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Amino acid discrimination by the nuclear encoded mitochondrial arginyl-tRNA synthetase of the larva of a bruchid beetle (Caryedes brasiliensis) from northwestern Costa Rica

Cited by 11 publications

References 55 publications

Detection of Inosine on Transfer RNAs without a Reverse Transcription Reaction

Detection of Inosine on Transfer RNAs without a Reverse Transcription Reaction

Molecular evidence for the evolution of the eukaryotic mitochondrial arginyl‐tRNA synthetase from the prokaryotic suborder Cystobacterineae

Identity elements for the aminoacylation of metazoan mitochondrial tRNA^Arghave been widely conserved throughout evolution and ensure the fidelity of the AGR codon reassignment

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Amino acid discrimination by the nuclear encoded mitochondrial arginyl-tRNA synthetase of the larva of a bruchid beetle (Caryedes brasiliensis) from northwestern Costa Rica

Cited by 11 publications

References 55 publications

Detection of Inosine on Transfer RNAs without a Reverse Transcription Reaction

Detection of Inosine on Transfer RNAs without a Reverse Transcription Reaction

Molecular evidence for the evolution of the eukaryotic mitochondrial arginyl‐tRNA synthetase from the prokaryotic suborder Cystobacterineae

Identity elements for the aminoacylation of metazoan mitochondrial tRNAArghave been widely conserved throughout evolution and ensure the fidelity of the AGR codon reassignment

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Identity elements for the aminoacylation of metazoan mitochondrial tRNA^Arghave been widely conserved throughout evolution and ensure the fidelity of the AGR codon reassignment