tRNA aminoacylation (Homo sapiens)
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Description
A single synthetase mediates the charging of all of the tRNA species specific for any one amino acid but, with three exceptions, glycine, lysine, and glutamine, the synthetase that catalyzes aminoacylation of mitochondrial tRNAs is encoded by a different gene than the one that acts on mitochondrial tRNAs. Both mitochondrial and cytosolic tRNA synthetase enzymes are encoded by genes in the nuclear genome.<p>A number of tRNA synthetases are known to have functions distinct from tRNA charging (reviewed by Park et al. 2005). Additionally, mutations in several of the tRNA synthetases, often affecting protein domains that are dispensable in vitro for aminoacyl tRNA synthesis, are associated with a diverse array of neurological and other diseases (Antonellis and Green 2008; Park et al. 2008). These findings raise interest into the role of these enzymes in human development and disease.<p></div>
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- Vilalta A, Donovan D, Wood L, Vogeli G, Yang DC.; ''Cloning, sequencing and expression of a cDNA encoding mammalian valyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Kaminska M, Shalak V, Mirande M.; ''The appended C-domain of human methionyl-tRNA synthetase has a tRNA-sequestering function.''; PubMed Europe PMC Scholia
- Spencer AC, Heck A, Takeuchi N, Watanabe K, Spremulli LL.; ''Characterization of the human mitochondrial methionyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Burbaum JJ, Schimmel P.; ''Structural relationships and the classification of aminoacyl-tRNA synthetases.''; PubMed Europe PMC Scholia
- O'Hanlon TP, Raben N, Miller FW.; ''A novel gene oriented in a head-to-head configuration with the human histidyl-tRNA synthetase (HRS) gene encodes an mRNA that predicts a polypeptide homologous to HRS.''; PubMed Europe PMC Scholia
- Bullard JM, Cai YC, Spremulli LL.; ''Expression and characterization of the human mitochondrial leucyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Lamour V, Quevillon S, Diriong S, N'Guyen VC, Lipinski M, Mirande M.; ''Evolution of the Glx-tRNA synthetase family: the glutaminyl enzyme as a case of horizontal gene transfer.''; PubMed Europe PMC Scholia
- Park SG, Schimmel P, Kim S.; ''Aminoacyl tRNA synthetases and their connections to disease.''; PubMed Europe PMC Scholia
- Jordanova A, Irobi J, Thomas FP, Van Dijck P, Meerschaert K, Dewil M, Dierick I, Jacobs A, De Vriendt E, Guergueltcheva V, Rao CV, Tournev I, Gondim FA, D'Hooghe M, Van Gerwen V, Callaerts P, Van Den Bosch L, Timmermans JP, Robberecht W, Gettemans J, Thevelein JM, De Jonghe P, Kremensky I, Timmerman V.; ''Disrupted function and axonal distribution of mutant tyrosyl-tRNA synthetase in dominant intermediate Charcot-Marie-Tooth neuropathy.''; PubMed Europe PMC Scholia
- Shiba K, Ripmaster T, Suzuki N, Nichols R, Plotz P, Noda T, Schimmel P.; ''Human alanyl-tRNA synthetase: conservation in evolution of catalytic core and microhelix recognition.''; PubMed Europe PMC Scholia
- Edvardson S, Shaag A, Kolesnikova O, Gomori JM, Tarassov I, Einbinder T, Saada A, Elpeleg O.; ''Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia.''; PubMed Europe PMC Scholia
- Curbo S, Lagier-Tourenne C, Carrozzo R, Palenzuela L, Lucioli S, Hirano M, Santorelli F, Arenas J, Karlsson A, Johansson M.; ''Human mitochondrial pyrophosphatase: cDNA cloning and analysis of the gene in patients with mtDNA depletion syndromes.''; PubMed Europe PMC Scholia
- Fersht AR, Kaethner MM.; ''Mechanism of aminoacylation of tRNA. Proof of the aminoacyl adenylate pathway for the isoleucyl- and tyrosyl-tRNA synthetases from Escherichia coli K12.''; PubMed Europe PMC Scholia
- Fisher RA, Turner BM, Dorkin HL, Harris H.; ''Studies on human erythrocyte inorganic pyrophosphatase.''; PubMed Europe PMC Scholia
- Scheper GC, van der Klok T, van Andel RJ, van Berkel CG, Sissler M, Smet J, Muravina TI, Serkov SV, Uziel G, Bugiani M, Schiffmann R, Krägeloh-Mann I, Smeitink JA, Florentz C, Van Coster R, Pronk JC, van der Knaap MS.; ''Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation.''; PubMed Europe PMC Scholia
- Wolfe CL, Warrington JA, Davis S, Green S, Norcum MT.; ''Isolation and characterization of human nuclear and cytosolic multisynthetase complexes and the intracellular distribution of p43/EMAPII.''; PubMed Europe PMC Scholia
- Degoul F, Brulé H, Cepanec C, Helm M, Marsac C, Leroux J, Giegé R, Florentz C.; ''Isoleucylation properties of native human mitochondrial tRNAIle and tRNAIle transcripts. Implications for cardiomyopathy-related point mutations (4269, 4317) in the tRNAIle gene.''; PubMed Europe PMC Scholia
- Jorgensen R, Søgaard TM, Rossing AB, Martensen PM, Justesen J.; ''Identification and characterization of human mitochondrial tryptophanyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Baldwin AN, Berg P.; ''Transfer ribonucleic acid-induced hydrolysis of valyladenylate bound to isoleucyl ribonucleic acid synthetase.''; PubMed Europe PMC Scholia
- Antonellis A, Ellsworth RE, Sambuughin N, Puls I, Abel A, Lee-Lin SQ, Jordanova A, Kremensky I, Christodoulou K, Middleton LT, Sivakumar K, Ionasescu V, Funalot B, Vance JM, Goldfarb LG, Fischbeck KH, Green ED.; ''Glycyl tRNA synthetase mutations in Charcot-Marie-Tooth disease type 2D and distal spinal muscular atrophy type V.''; PubMed Europe PMC Scholia
- Park SG, Ewalt KL, Kim S.; ''Functional expansion of aminoacyl-tRNA synthetases and their interacting factors: new perspectives on housekeepers.''; PubMed Europe PMC Scholia
- Ling C, Yao YN, Zheng YG, Wei H, Wang L, Wu XF, Wang ED.; ''The C-terminal appended domain of human cytosolic leucyl-tRNA synthetase is indispensable in its interaction with arginyl-tRNA synthetase in the multi-tRNA synthetase complex.''; PubMed Europe PMC Scholia
- Moor N, Linshiz G, Safro M.; ''Cloning and expression of human phenylalanyl-tRNA synthetase in Escherichia coli: comparative study of purified recombinant enzymes.''; PubMed Europe PMC Scholia
- Yang XL, Otero FJ, Skene RJ, McRee DE, Schimmel P, Ribas de Pouplana L.; ''Crystal structures that suggest late development of genetic code components for differentiating aromatic side chains.''; PubMed Europe PMC Scholia
- Beaulande M, Tarbouriech N, Härtlein M.; ''Human cytosolic asparaginyl-tRNA synthetase: cDNA sequence, functional expression in Escherichia coli and characterization as human autoantigen.''; PubMed Europe PMC Scholia
- Vincent C, Tarbouriech N, Härtlein M.; ''Genomic organization, cDNA sequence, bacterial expression, and purification of human seryl-tRNA synthase.''; PubMed Europe PMC Scholia
- Pan F, Lee HH, Pai SH, Lo KY.; ''Purification and subunit structure studies of human placental threonyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Yu Y, Liu Y, Shen N, Xu X, Xu F, Jia J, Jin Y, Arnold E, Ding J.; ''Crystal structure of human tryptophanyl-tRNA synthetase catalytic fragment: insights into substrate recognition, tRNA binding, and angiogenesis activity.''; PubMed Europe PMC Scholia
- Escalante C, Yang DC.; ''Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix.''; PubMed Europe PMC Scholia
- Bange FC, Flohr T, Buwitt U, Böttger EC.; ''An interferon-induced protein with release factor activity is a tryptophanyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T.; ''Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit.''; PubMed Europe PMC Scholia
- Pynes GD, Younathan ES.; ''Purification and some properties of inorganic pyrophosphatase from human erythrocytes.''; PubMed Europe PMC Scholia
- Rubin BY, Anderson SL, Xing L, Powell RJ, Tate WP.; ''Interferon induces tryptophanyl-tRNA synthetase expression in human fibroblasts.''; PubMed Europe PMC Scholia
- Davidson E, Caffarella J, Vitseva O, Hou YM, King MP.; ''Isolation of two cDNAs encoding functional human cytoplasmic cysteinyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Baldwin AN, Berg P.; ''Purification and properties of isoleucyl ribonucleic acid synthetase from Escherichia coli.''; PubMed Europe PMC Scholia
- Thuillier L.; ''Purification and kinetic properties of human erythrocyte Mg2+-dependent inorganic pyrophosphatase.''; PubMed Europe PMC Scholia
- Lee JW, Beebe K, Nangle LA, Jang J, Longo-Guess CM, Cook SA, Davisson MT, Sundberg JP, Schimmel P, Ackerman SL.; ''Editing-defective tRNA synthetase causes protein misfolding and neurodegeneration.''; PubMed Europe PMC Scholia
- Bullard JM, Cai YC, Demeler B, Spremulli LL.; ''Expression and characterization of a human mitochondrial phenylalanyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Kaiser E, Hu B, Becher S, Eberhard D, Schray B, Baack M, Hameister H, Knippers R.; ''The human EPRS locus (formerly the QARS locus): a gene encoding a class I and a class II aminoacyl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M.; ''Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS.''; PubMed Europe PMC Scholia
- Fersht AR, Kaethner MM.; ''Enzyme hyperspecificity. Rejection of threonine by the valyl-tRNA synthetase by misacylation and hydrolytic editing.''; PubMed Europe PMC Scholia
- Yokogawa T, Shimada N, Takeuchi N, Benkowski L, Suzuki T, Omori A, Ueda T, Nishikawa K, Spremulli LL, Watanabe K.; ''Characterization and tRNA recognition of mammalian mitochondrial seryl-tRNA synthetase.''; PubMed Europe PMC Scholia
- Sang Lee J, Gyu Park S, Park H, Seol W, Lee S, Kim S.; ''Interaction network of human aminoacyl-tRNA synthetases and subunits of elongation factor 1 complex.''; PubMed Europe PMC Scholia
- Shiba K, Stello T, Motegi H, Noda T, Musier-Forsyth K, Schimmel P.; ''Human lysyl-tRNA synthetase accepts nucleotide 73 variants and rescues Escherichia coli double-defective mutant.''; PubMed Europe PMC Scholia
- Antonellis A, Green ED.; ''The role of aminoacyl-tRNA synthetases in genetic diseases.''; PubMed Europe PMC Scholia
History
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External references
DataNodes
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Name | Type | Database reference | Comment |
---|---|---|---|
AARS | Protein | P49588 (Uniprot-TrEMBL) | |
AARS2 | Protein | Q5JTZ9 (Uniprot-TrEMBL) | |
AMP | Metabolite | 16027 (ChEBI) | |
ATP | Metabolite | 15422 (ChEBI) | |
Ala-tRNA
(Ala) | Metabolite | 17732 (ChEBI) | |
Arg-tRNA
(Arg) | Metabolite | 18366 (ChEBI) | |
Asn-tRNA
(Asn) | Metabolite | 29265 (ChEBI) | |
Asp-tRNA
(Asp) | Metabolite | 29158 (ChEBI) | |
CARS
dimer | Complex | REACT_17681 (Reactome) | |
CARS2 | Protein | Q9HA77 (Uniprot-TrEMBL) | |
Cys-tRNA
(Cys) | Metabolite | 29152 (ChEBI) | |
DARS2
dimer | Complex | REACT_15709 (Reactome) | |
EARS2 | Protein | Q5JPH6 (Uniprot-TrEMBL) | |
FARS
A2B2 tetramer | Complex | REACT_16104 (Reactome) | |
FARS2 | Protein | O95363 (Uniprot-TrEMBL) | |
GARS
dimer | Complex | REACT_15693 (Reactome) | |
GARS dimer | Complex | REACT_17609 (Reactome) | |
Gln-tRNA
(Gln) | Metabolite | 29166 (ChEBI) | |
Glu-tRNA
(Glu) | Metabolite | 29157 (ChEBI) | |
Gly-tRNA
(Gly) | Metabolite | 29156 (ChEBI) | |
Glycine | Metabolite | 15428 (ChEBI) | |
H2O | Metabolite | 15377 (ChEBI) | |
HARS | Protein | P12081 (Uniprot-TrEMBL) | |
HARS2 | Protein | P49590 (Uniprot-TrEMBL) | |
His-tRNA
(His) | Metabolite | 29155 (ChEBI) | |
IARS2 | Protein | Q9NSE4 (Uniprot-TrEMBL) | |
Ile-tRNA
(Ile) | Metabolite | 29160 (ChEBI) | |
KARS
dimer | Complex | REACT_15848 (Reactome) | |
L-Alanine | Metabolite | 16977 (ChEBI) | |
L-Arginine | Metabolite | 16467 (ChEBI) | |
L-Asparagine | Metabolite | 17196 (ChEBI) | |
L-Aspartate | Metabolite | 17053 (ChEBI) | |
L-Glutamate | Metabolite | 16015 (ChEBI) | |
L-Glutamine | Metabolite | 18050 (ChEBI) | |
L-Histidine | Metabolite | 15971 (ChEBI) | |
L-Isoleucine | Metabolite | 17191 (ChEBI) | |
L-Leucine | Metabolite | 15603 (ChEBI) | |
L-Lysine | Metabolite | 18019 (ChEBI) | |
L-Methionine | Metabolite | 16643 (ChEBI) | |
L-Phenylalanine | Metabolite | 17295 (ChEBI) | |
L-Proline | Metabolite | 17203 (ChEBI) | |
L-Threonine | Metabolite | 16857 (ChEBI) | |
L-Tryptophan | Metabolite | 16828 (ChEBI) | |
L-Tyrosine | Metabolite | 17895 (ChEBI) | |
L-Valine | Metabolite | 16414 (ChEBI) | |
L-cysteine | Metabolite | 17561 (ChEBI) | |
L-serine | Metabolite | 17115 (ChEBI) | |
LARS2 | Protein | Q15031 (Uniprot-TrEMBL) | |
Leu-tRNA
(Leu) | Metabolite | 16624 (ChEBI) | |
Lys-tRNA
(Lys) | Metabolite | 16047 (ChEBI) | |
MARS2 | Protein | Q96GW9 (Uniprot-TrEMBL) | |
Magnesium | Metabolite | 18420 (ChEBI) | |
Met-tRNA
(Met) | Metabolite | 16635 (ChEBI) | |
Mg++ | Metabolite | 18420 (ChEBI) | |
NARS | Protein | O43776 (Uniprot-TrEMBL) | |
NARS2 | Protein | Q96I59 (Uniprot-TrEMBL) | |
Orthophosp
hate | Metabolite | 18367 (ChEBI) | |
PARS2 | Protein | Q7L3T8 (Uniprot-TrEMBL) | |
PPA1
dimer | Complex | REACT_3635 (Reactome) | |
PPA2
dimer | Complex | REACT_21920 (Reactome) | |
Phe-tRNA
(Phe) | Metabolite | 29153 (ChEBI) | |
Phe-tRNA(Phe) | Metabolite | 29153 (ChEBI) | |
Pro-tRNA
(Pro) | Metabolite | 29154 (ChEBI) | |
QARS | Protein | P47897 (Uniprot-TrEMBL) | |
RARS2 | Protein | Q5T160 (Uniprot-TrEMBL) | |
SARS
dimer | Complex | REACT_18078 (Reactome) | |
SARS2
dimer | Complex | REACT_15712 (Reactome) | |
Ser-tRNA
(Ser) | Metabolite | 29162 (ChEBI) | |
TARS
dimer | Complex | REACT_16019 (Reactome) | |
TARS2 | Protein | Q9BW92 (Uniprot-TrEMBL) | |
Thr-tRNA
(Thr) | Metabolite | 29163 (ChEBI) | |
Trp-tRNA
(Trp) | Metabolite | 29159 (ChEBI) | |
Tyr-tRNA
(Tyr) | Metabolite | 29161 (ChEBI) | |
VARS | Protein | P26640 (Uniprot-TrEMBL) | |
VARS2 | Protein | Q5ST30 (Uniprot-TrEMBL) | |
Val-tRNA
(Val) | Metabolite | 29164 (ChEBI) | |
WARS
dimer | Complex | REACT_15987 (Reactome) | |
WARS2 | Protein | Q9UGM6 (Uniprot-TrEMBL) | |
YARS
dimer | Complex | REACT_16005 (Reactome) | |
YARS2
dimer | Complex | REACT_18046 (Reactome) | |
aminoacyl-tRNA
synthetase multienzyme complex | Complex | REACT_15869 (Reactome) | |
glycine | Metabolite | 15428 (ChEBI) | |
pyrophosp
hate | Metabolite | 29888 (ChEBI) | |
tRNA(Ala) | Metabolite | 17732 (ChEBI) | |
tRNA(Arg) | Metabolite | 29171 (ChEBI) | |
tRNA(Asn) | Metabolite | 29172 (ChEBI) | |
tRNA(Asp) | Metabolite | 29186 (ChEBI) | |
tRNA(Cys) | Metabolite | 29167 (ChEBI) | |
tRNA(Gln) | Metabolite | 29168 (ChEBI) | |
tRNA(Glu) | Metabolite | 29175 (ChEBI) | |
tRNA(Gly) | Metabolite | 29176 (ChEBI) | |
tRNA(His) | Metabolite | 29178 (ChEBI) | |
tRNA(Ile) | Metabolite | 29174 (ChEBI) | |
tRNA(Leu) | Metabolite | 29169 (ChEBI) | |
tRNA(Lys) | Metabolite | 29185 (ChEBI) | |
tRNA(Met) | Metabolite | 29173 (ChEBI) | |
tRNA(Phe) | Metabolite | 29184 (ChEBI) | |
tRNA(Pro) | Metabolite | 29177 (ChEBI) | |
tRNA(Ser) | Metabolite | 29179 (ChEBI) | |
tRNA(Thr) | Metabolite | 29180 (ChEBI) | |
tRNA(Trp) | Metabolite | 29181 (ChEBI) | |
tRNA(Tyr) | Metabolite | 29182 (ChEBI) | |
tRNA(Val) | Metabolite | 29183 (ChEBI) |