APhaseolus vulgaris mitochondrial tRNALeu is identical to its cytoplasmic counterpart: sequencing andin vivo transcription of the gene corresponding to the cytoplasmic tRNALeu

Green, Gaynor A.; Marechal, Laurence; Weil, Jacques-Henry; Guillemaut, Pierre

doi:10.1007/bf00014182

Cited by 57 publications

(57 citation statements)

References 25 publications

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“…In yeast, two different tRNA NAA Leu species have either a modified U (40) or a modified C (41) in the wobble position, restricting base pairing to either UUA or UUG codons, respectively. The same situation probably also exists in mammals (42) and plants (1,25). Judging by the results of direct sequencing of the wheat Leu3 and Leu4 tRNAs, the wobble nucleoside in both species also appears to be modified.…”

Section: Primary and Secondary Structures Of Sequenced Trnas-mentioning

confidence: 85%

“…In flowering plants (angiosperms), all of the codons of the canonical genetic code are represented in the protein genes encoded by mtDNA, 1 yet the mitochondrial genome appears to specify fewer than the 23-24 or 33 tRNAs minimally required to read these codons by either expanded or standard wobble base pairing, respectively. This observation, coupled with the identification of cytosolic-like tRNAs in mitochondrial RNA preparations of bean (1), wheat (2), and potato (3), suggests that tRNAs must be imported into angiosperm mitochondria (4 -6), as they are into the mitochondria of many unicellular eukaryotes (7).…”

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confidence: 99%

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Identification and Structural Characterization of Nucleus-encoded Transfer RNAs Imported into Wheat Mitochondria

Glover

Spencer

Gray

2001

Journal of Biological Chemistry

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Despite its large size (200 -2400 kilobase pairs), the mitochondrial genome of angiosperms does not encode the minimal set of tRNAs required to support mitochondrial protein synthesis. Here we report the identification of cytosolic-like tRNAs in wheat mitochondria using a method involving quantitative hybridization to distinguish among three tRNA classes: (i) those encoded by mitochondrial DNA (mtDNA) and localized in mitochondria, (ii) those encoded by nuclear DNA and located in the cytosol, and (iii) those encoded by nuclear DNA and found in both the cytosol and mitochondria. The latter class comprises tRNA species that are considered to be imported into mitochondria to compensate for the deficiency of mtDNA-encoded tRNAs. In a comprehensive survey of the wheat mitochondrial tRNA population, we identified 14 such imported tRNAs, the structural characterization of which is presented here. These imported tRNAs complement 16 mtDNA-encoded tRNAs, for a total of at least 30 distinct tRNA species in wheat mitochondria. Considering differences in the set of mtDNA-encoded and imported tRNAs in the mitochondria of various land plants, the import system must be able to adapt relatively rapidly over evolutionary time with regard to the particular cytosolic-like tRNAs that are brought into mitochondria.

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Section: Primary and Secondary Structures Of Sequenced Trnas-mentioning

confidence: 85%

mentioning

confidence: 99%

Identification and Structural Characterization of Nucleus-encoded Transfer RNAs Imported into Wheat Mitochondria

Glover

Spencer

Gray

2001

Journal of Biological Chemistry

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“…Most of the imported tRNAs identified in diverse organisms function in cytosolic translation in addition to mitochondrial translation (Suyama and Hamada 1976;Green et al 1987;Mar6chal-Drouard et al 1988;Hancock and Hajduk 1990;Schneider et al 1994;Rusconi and Cech 1996). This implies that a branch point exists in most tRNA import pathways at which molecules to be imported are partitioned either to the cytosol for cytosolic translation or to mitochondria for mitochondrial translation.…”

Section: T R N a Import In Tetrahymenamentioning

confidence: 99%

The anticodon is the signal sequence for mitochondrial import of glutamine tRNA in Tetrahymena.

Rusconi¹,

Cech²

1996

Genes Dev.

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The import of nuclear-encoded RNAs into mitochondria is required for proper mitochondrial function in most organisms. However, the mechanisms used to achieve RNA import are largely unknown. In particular, the RNA elements that direct import have not been identified in any organism. In Tetrahymena, only one of three nuclear-encoded glutamine accepting tRNAs is imported into mitochondria. We transform Tetrahymena with marked glutamine tRNAs and quantitate their level of accumulation in mitochondria. Of several isostructural nucleotide substitutions tested, alteration of the anticodon sequence uniquely abolishes import. Furthermore, substitution of a single anticodon nucleotide (UUA-,UUG) confers import on a normally nonimported glutamine tRNA. Thus, the anticodon functions as a mitochondrial localization signal and is both necessary and sufficient for tRNA import. Given the prior evidence that neither the cytoplasmic nor the mitochondrial glutaminyl-tRNA synthetase distinguishes between the imported and nonimported glutamine tRNAs with respect to aminoacylation, we propose that some mitochondrial import factor distinct from a synthetase recognizes the anticodon of the imported glutamine tRNA.

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“…None of them contains an intron, including a Phaseolus tRNALe" gene with a CAA anticodon (Green et al, 1987), although this gene carries an intron in other eukaryotes like yeast and Drosophila (Sprinzl et al, 1991). The only exception is a tRNAMe' gene from Glycine max which has an 1 1-bp long intron (Waldron et al, 1985).…”

Section: Discussionmentioning

confidence: 99%

Intron excision from tRNA precursors by plant splicing endonuclease requires unique features of the mature tRNA domain

Stange

Beier

1992

European Journal of Biochemistry

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It has been proposed that yeast and Xenopus splicing endonucleases initially recognize features in the mature tRNA domain common to all tRNA species and that the sequence and structure of the intron are only minor determinants of splice-site selection. In accordance with this postulation, we show that yeast endonuclease splices heterologous pre-tRNATY' species from vertebrates and plants which differ in their mature domains and intron secondary structures. In contrast, wheat germ splicing endonuclease displays a pronounced preference for homologous pre-tRNA species; an extensive study of heterologous substrates revealed that neither yeast pre-tRNA species specific for leucine, serine, phenylalanine and tyrosine nor human and Xenopus pre-tRNATYr species were spliced. In order to identify the elements essential for pre-tRNA splicing in plants, we constructed chimeric genes coding for tRNA precursors with a plant intron secondary structure and with mature tRNATy' domains from yeast and Xenopus, respectively. The chimeric pre-tRNA comprising the mature tRNATyr domain from Xenopus was spliced efficiently in wheat germ extract, whereas the chimeric construct containing the mature tRNATyr domain from yeast was not spliced at all. These data indicate that intron secondary structure contributes to the specificity of plant splicing endonuclease and that unique features of the mature tRNA domain play a dominant role in enzyme-substrate recognition. We further investigated the influence of specific nucleotides in the mature domain on splicing by generating a number of mutated pre-tRNA species. Our results suggest that nucleotides located in the D stem, i.e. in the center of the pre-tRNA molecule, are recognition points for plant splicing endonuclease.

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APhaseolus vulgaris mitochondrial tRNALeu is identical to its cytoplasmic counterpart: sequencing andin vivo transcription of the gene corresponding to the cytoplasmic tRNALeu

Cited by 57 publications

References 25 publications

Identification and Structural Characterization of Nucleus-encoded Transfer RNAs Imported into Wheat Mitochondria

Identification and Structural Characterization of Nucleus-encoded Transfer RNAs Imported into Wheat Mitochondria

The anticodon is the signal sequence for mitochondrial import of glutamine tRNA in Tetrahymena.

Intron excision from tRNA precursors by plant splicing endonuclease requires unique features of the mature tRNA domain

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