<i>Saccharomyces cerevisiae</i> imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondrion

Rinehart, Jesse; Krett, Bethany; Rubio, Mary Anne T.; Alfonzo, Juan D.; Söll, Dieter

doi:10.1101/gad.1269305

Cited by 100 publications

(106 citation statements)

References 47 publications

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“…One could suggest therefore that inhibited or perturbed translation (appearance of additional translation products) is due to a decrease of imported tRK1. This is in agreement with our previous observation of suppression of a mtDNA mutation by imported tRNAs (Kolesnikova et al 2000) and with a more recent hypothesis suggesting the need of several cytoplasmic tRNAs to provide a complete decoding in yeast mitochondria (Rinehart et al 2005). It may occur that we obtained here the first evidence that, at least at higher temperature, tRK1 is recruited by mitochondrial translation machinery.…”

Section: Enolase Another Protein With Multiple Functionssupporting

confidence: 82%

“…targeted, tRNA Gln (Rinehart et al 2005) and tRNA Lys CUU (further referred to as tRK1) (Martin et al 1979), whose import appears to proceed by different mechanisms. Mitochondrial functions of tRK1 are not completely clear, although our previous results demonstrated that its mutant versions are functional in mitochondrial translation, since they are able to suppress a nonsense mutation in mitochondrial DNA-localized gene (Kolesnikova et al 2000).…”

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confidence: 99%

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A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

Entelis¹,

Brandina²,

Kamenski³

et al. 2006

Genes Dev.

158

134

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In many organisms, mitochondria import nuclear DNA-encoded small RNAs. In yeast Saccharomyces cerevisiae, one out of two cytoplasmic isoacceptor tRNAs Lys is partially addressed into the organelle. Mitochondrial targeting of this tRNA was shown to depend on interaction with the precursor of mitochondrial lysyl-tRNA synthetase, preMsk1p. However, preMsk1p alone was unable to direct tRNA targeting, suggesting the existence of additional protein factor(s). Here, we identify the glycolytic enzyme, enolase, as such a factor. We demonstrate that recombinant enolase and preMSK1p are sufficient to direct tRNA import in vitro and that depletion of enolase inhibits tRNA import in vivo. Enzymatic and tRNA targeting functions of enolase appear to be independent. Three newly characterized properties of the enolase can be related to its novel function: (1) specific affinity to the imported tRNA, (2) the ability to facilitate formation of the complex between preMsk1p and the imported tRNA, and (3) partial targeting toward the mitochondrial outer membrane. We propose a model suggesting that the cell exploits mitochondrial targeting of the enolase in order to address the tRNA toward peri-mitochondrially synthesized preMsk1p. Our results indicate an alternative molecular chaperone function of glycolytic enzyme enolase in tRNA mitochondrial targeting.

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Section: Enolase Another Protein With Multiple Functionssupporting

confidence: 82%

mentioning

confidence: 99%

A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

Entelis¹,

Brandina²,

Kamenski³

et al. 2006

Genes Dev.

158

134

View full text Add to dashboard Cite

show abstract

“…For glutamine (Gln), only one expressed cytosolic GlnRS was found. This observation is in accordance with the fact that Gln-tRNA Gln formation was shown to occur by transamidation in chloroplasts, and led to the suggestion that the same route of Gln-tRNA synthesis is also prevalent in mitochondria, although it has been shown in yeast that the cytosolic GlnRS is imported into mitochondria and is involved in mitochondrial Gln-tRNA Gln formation (17).…”

Section: Forty-five Expressed Aars Genes Were Found In the A Thalianasupporting

confidence: 55%

Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana

Duchêne

Giritch

Hoffmann

et al. 2005

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

238

232

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In plants, protein synthesis occurs in the cytosol, mitochondria, and plastids. Each compartment requires a full set of tRNAs and aminoacyl-tRNA synthetases. We have undertaken a systematic analysis of the targeting of organellar aminoacyl-tRNA synthetases in the model plant Arabidopsis thaliana. Dual targeting appeared to be a general rule. Among the 24 identified organellar aminoacyltRNA synthetases (aaRSs), 15 (and probably 17) are shared between mitochondria and plastids, and 5 are shared between cytosol and mitochondria (one of these aaRSs being present also in chloroplasts). Only two were shown to be uniquely chloroplastic and none to be uniquely mitochondrial. Moreover, there are no examples where the three aaRS genes originating from the three ancestral genomes still coexist. These results indicate that extensive exchange of aaRSs has occurred during evolution and that many are now shared between two or even three compartments. The findings have important implications for studies of the translation machinery in plants and on protein targeting and gene transfer in general.GFP ͉ mitochondria ͉ plastids ͉ protein targeting ͉ translation

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“…does not form Glu-tRNA Gln ) and the cytoplasmic GlnRS is present in the yeast mitochondria suggests a Glu-AdT is also not required in the organelle. 60 The conservation of the important residues in Pet112 for the kinase activity of GatB and GatE indicates a catalytic role for the enzyme in the cell.…”

Section: Alternative Function(s) For the Gatcab Subunit?mentioning

confidence: 99%

On the Evolution of the tRNA-Dependent Amidotransferases, GatCAB and GatDE

Sheppard

Söll

2008

Journal of Molecular Biology

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SummaryGlutaminyl-tRNA synthetase and asparaginyl-tRNA synthetase evolved from glutamyl-tRNA synthetase and aspartyl-tRNA synthetase, respectively, after the split in the last universal communal ancestor (LUCA). Glutaminyl-tRNA Gln and asparaginyl-tRNA Asn were likely formed in LUCA by amidation of the mischarged species, glutamyl-tRNA Gln and aspartyl-tRNA Asn , by tRNA-dependent amidotransferases as is still the case in most bacteria and all known archaea. The amidotransferase GatCAB is found in both domains of life while the heterodimeric amidotransferase, GatDE, is found only in Archaea. The GatB and GatE subunits belong to a unique protein family with Pet112 that is encoded in the nuclear genomes of numerous eukaryotes. GatE was thought to have evolved from GatB after the emergence of the modern lines of decent. Our phylogenetic analysis though places the split between GatE and GatB prior to the phylogenetic divide between Bacteria and Archaea and Pet112 to be of mitochondrial origin. In addition, GatD appears to have emerged prior to the bacterialarchaeal phylogenetic divide. Thus, while GatDE is an archaeal signature protein it likely was present in LUCA together with GatCAB. Archaea retained both amidotransferases while Bacteria emerged with only GatCAB. The presence of GatDE has favored a unique archaeal tRNA Gln that may be preventing acquisition of glutaminyl-tRNA synthetase in Archaea. Archaeal GatCAB on the other hand has not favored a distinct tRNA Asn suggesting tRNA Asn recognition is not a major barrier to the retention of asparaginyl-tRNA synthetase in more Archaea.

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Saccharomyces cerevisiae imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondrion

Cited by 100 publications

References 47 publications

A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae

Dual targeting is the rule for organellar aminoacyl-tRNA synthetases in Arabidopsis thaliana

On the Evolution of the tRNA-Dependent Amidotransferases, GatCAB and GatDE

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