The strange evolutionary history of plant mitochondrial tRNAs and their aminoacyl-tRNA synthetases

Small, Ian; Akashi, Kinya; Chapron, A.; Dietrich, André; Duchêne, Anne‐Marie; Lancelin, Dominique; Maréchal-Drouard, Laurence; Menand, Benoît; Mireau, Hakim; Moudden, Y.; Ovesná, Jaroslava; Peeters, Nemo; Sakamoto, Wataru; Souciet, Ginette; Wintz, Henri

doi:10.1093/jhered/90.3.333

Cited by 34 publications

(22 citation statements)

References 31 publications

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“…However, as in other eukaryotes, the situation is more complicated, as there are several cases where one gene has replaced the function of another because its gene product is dual-targeted to two compartments. Dual-targeting to the cytosol and mitochondria was shown for Arabidopsis alanyl-tRNA synthetase (Mireau et al 1996) and is probably also the case for several other plant aaRSs (Small et al 1999). Dualtargeting is also possible to mitochondria and plastids, as demonstrated for Arabidopsis histidyl-tRNA ) and methionyl-tRNA (Menand et al 1998) synthetases.…”

Section: Introductionmentioning

confidence: 71%

“…In plants, the situation is a little different for two major reasons: the acquisition of plastids has provided an influx of new tRNA and aaRS genes, and the mitochondrial translation system has diverged very little from the eubacterial standard. This has allowed considerable sharing of aaRSs and tRNAs between compartments (Small et al 1999). In particular, plant mitochondria contain a number of tRNAs expressed from insertions of plastid DNA in the mitochondrial genome.…”

Section: Dual-targetingmentioning

confidence: 99%

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Duplication and Quadruplication of Arabidopsis thaliana Cysteinyl- and Asparaginyl-tRNA Synthetase Genes of Organellar Origin

et al. 2000

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Abstract. Two cysteinyl-tRNA synthetases (CysRS) and four asparaginyl-tRNA synthetases (AsnRS) from Arabidopsis thaliana were characterized from genome sequence data, EST sequences, and RACE sequences. For one CysRS and one AsnRS, sequence alignments and prediction programs suggested the presence of an N-terminal organellar targeting peptide. Transient expression of these putative targeting sequences joined to jellyfish green fluorescent protein (GFP) demonstrated that both presequences can efficiently dual-target GFP to mitochondria and plastids. The other CysRS and AsnRSs lack targeting sequences and presumably aminoacylate cytosolic tRNAs. Phylogenetic analysis suggests that the four AsnRSs evolved by repeated duplication of a gene transferred from an ancestral plastid and that the CysRSs also arose by duplication of a transferred organelle gene (possibly mitochondrial). These case histories are the best examples to date of capture of organellar aminoacyltRNA synthetases by the cytosolic protein synthesis machinery.

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Section: Introductionmentioning

confidence: 71%

Section: Dual-targetingmentioning

confidence: 99%

Duplication and Quadruplication of Arabidopsis thaliana Cysteinyl- and Asparaginyl-tRNA Synthetase Genes of Organellar Origin

et al. 2000

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“…Approximately 40 examples of dual-targeted proteins of the thousands of organellar-imported proteins have been identified in A. thaliana, but half of these proteins correspond to aaRSs (11). Eighteen of 24 identified A. thaliana organellar aaRSs are shared between mitochondria and chloroplasts (8,18). The dual localization of GatCAB gives an example of cross-compartment sharing of enzymes involved in aa-tRNA synthesis.…”

Section: Glnrs Mito Nd-glursmentioning

confidence: 99%

Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial and chloroplastic Gln-tRNA ^Gln synthesis in plants

Pujol

Bailly

Kern

et al. 2008

Proc. Natl. Acad. Sci. U.S.A.

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Aminoacyl-tRNAs are generally formed by direct attachment of an amino acid to tRNAs by aminoacyl-tRNA synthetases, but Gln-tRNA is an exception to this rule. Gln-tRNA Gln is formed by this direct pathway in the eukaryotic cytosol and in protists or fungi mitochondria but is formed by an indirect transamidation pathway in most of bacteria, archaea, and chloroplasts. We show here that the formation of Gln-tRNA Gln is also achieved by the indirect pathway in plant mitochondria. The mitochondrial-encoded tRNA Gln , which is the only tRNA Gln present in mitochondria, is first charged with glutamate by a nondiscriminating GluRS, then is converted into Gln-tRNA Gln by a tRNA-dependent amidotransferase (AdT). The three subunits GatA, GatB, and GatC are imported into mitochondria and assemble into a functional GatCAB AdT. Moreover, the mitochondrial pathway of Gln-tRNA Gln formation is shared with chloroplasts as both the GluRS, and the three AdT subunits are dual-imported into mitochondria and chloroplasts.amidation ͉ aminoacylation ͉ GatCAB ͉ glutamyl-tRNA synthetase ͉ protein trafficking

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“…Although some plants (e.g. Physcomitrella , Oryza and Vitis ) encode one or both of these isoacceptors, with a different sequence, on their mitochondrial genomes, others rely on the import of cytoplasmic tRNAs [24]. There are no data available concerning the mitochondrial genome of soybean.…”

Section: Resultsmentioning

confidence: 99%

“…The initial experimental demonstration of import into chloroplasts [22] has been augmented by reverse genetic screening data also suggesting mitochondrial import [23]. Thus, a single arginyl-tRNA synthetase must recognize not only the nuclear-encoded cognate tRNAs, but also the prokaryote-like plastid-encoded tRNAs and, in some plants [24], the distinct mitochondria-encoded tRNA Arg isoacceptors; a total of nine tRNAs with differing primary structure that are highly conserved between plant species (http://gtrnadb.ucsc.edu/). A sequence alignment of all isodecoders from nine plants corresponding to these tRNA Arg substrates (and ignoring universally conserved nucleotides and degenerate conservations) localizes five conserved bases and three conserved base pairs that are candidate identity elements.…”

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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The strange evolutionary history of plant mitochondrial tRNAs and their aminoacyl-tRNA synthetases

Cited by 34 publications

References 31 publications

Duplication and Quadruplication of Arabidopsis thaliana Cysteinyl- and Asparaginyl-tRNA Synthetase Genes of Organellar Origin

Duplication and Quadruplication of Arabidopsis thaliana Cysteinyl- and Asparaginyl-tRNA Synthetase Genes of Organellar Origin

Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial and chloroplastic Gln-tRNA ^Gln synthesis in plants

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

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The strange evolutionary history of plant mitochondrial tRNAs and their aminoacyl-tRNA synthetases

Cited by 34 publications

References 31 publications

Duplication and Quadruplication of Arabidopsis thaliana Cysteinyl- and Asparaginyl-tRNA Synthetase Genes of Organellar Origin

Duplication and Quadruplication of Arabidopsis thaliana Cysteinyl- and Asparaginyl-tRNA Synthetase Genes of Organellar Origin

Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial and chloroplastic Gln-tRNA Gln synthesis in plants

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

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Dual-targeted tRNA-dependent amidotransferase ensures both mitochondrial and chloroplastic Gln-tRNA ^Gln synthesis in plants

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