Abstract
Transfer RNAs (tRNAs) and aminoacyl-tRNA synthetases (aaRSs) are key actors in all translation machineries. AaRSs aminoacylate cognate tRNAs with a specific amino acid that is transferred to the growing protein chain on the ribosome. Mammalian mitochondria possess their own translation machinery for the synthesis of 13 proteins only, all subunits of the respiratory chain complexes involved in the synthesis of ATP. While 22 tRNAs and two ribosomal RNAs are also coded by the mitochondrial genome, aaRSs are nuclear encoded and become imported. The fact that the two cellular genomes, nuclear and mitochondrial, evolve at different rates raises numerous questions as to the co-evolution of partner macromolecules. Herein we review the present state-of-the-art on structural, biophysical, and functional peculiarities of mammalian mitochondrial tRNAs and aaRSs, and of their partnership in their wild-type state. Then, we oppose this mitochondrial “order” to the “disorder” generated by the presence of a variety of mutations occurring in the corresponding human genes that have been correlated to an increasing number of diseases. So far, more than 230 mutations in mitochondrial tRNA genes and a rapidly growing number of mutations in mitochondrial aaRS genes have been reported as causative of a large variety of pathologies. The molecular incidence of mutations on structural, biophysical and functional properties of the related macromolecules will be summarized. Mutations in mitochondrial tRNA genes lead to complex mosaic effects with a major impact on tRNA structure. Some mutations affecting mitochondrial aaRS genes do not interfere with the housekeeping aminoacylation activity, suggesting that mitochondrial aaRSs, alike cytosolic aaRSs are involved in other processes than translation. This opens new research lines.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
References
Alfonzo JD, Söll D (2009) Mitochondrial tRNA import—the challenge to understand has just begun. Biol Chem 390:717–722
Anderson S, Bankier AT, Barrel BG, de Bruijn MHL, Coulson AR, Drouin J, Eperon JC, Nierlich DP, Roe BA, Sanger F, Schreier PH, Smith AJH, Staden R, Young IG (1981) Sequence and organization of the human mitochondrial genome. Nature 290:457–465
Arcari P, Brownlee GG (1980) The nucleotide sequence of a small (3S) seryl-tRNA (anticodon GCU) from beef heart mitochondria. Nucleic Acids Res 8:5207–5212
Bayat V, Thiffault I, Jaiswal M, Tétreault M, Donti T, Sasarman F, Bernard G, Demers-Lamarche J, Dicaire MJ, Mathieu J, Vanasse M, Bouchard JP, Rioux MF, Lourenco CM, Li Z, Haueter C, Shoubridge EA, Graham BH, Brais B, Bellen HJ (2012) Mutations in the mitochondrial methionyl-tRNA synthetase cause a neurodegenerative phenotype in flies and a recessive ataxia (ARSAL) in humans. PLoS Biol 10:e1001288
Belostotsky R, Ben-Shalom E, Rinat C, Becker-Cohen R, Feinstein S, Zeligson S, Segel R, Elpeleg O, Nassar S, Frishberg Y (2011) Mutations in the mitochondrial seryl-tRNA synthetase cause hyperuricemia, pulmonary hypertension, renal failure in infancy and alkalosis, HUPRA syndrome. Am J Hum Genet 88:193–200
Bernt M, Donath A, Jühling F, Externbrink F, Florentz C, Fritzsch G, Pütz J, Middendorf M, Stadler PF (2012) MITOS: improved de novo metazoan mitochondrial genome annotation. Mol Phylogenet Evol [Epub ahead of print]
Bonnefond L, Fender A, Rudinger-Thirion J, Giegé R, Florentz C, Sissler M (2005a) Toward the full set of human mitochondrial aminoacyl-tRNA synthetases: characterization of AspRS and TyrRS. Biochemistry 44:4805–4816
Bonnefond L, Frugier M, Giegé R, Rudinger-Thirion J (2005b) Human mitochondrial TyrRS disobeys the tyrosine idenity rules. RNA 11:558–562
Bonnefond L, Frugier M, Touzé E, Lorber B, Florentz C, Giegé R, Sauter C, Rudinger-Thirion J (2007) Crystal structure of human mitochondrial tyrosyl-tRNA synthetase reveals common and idiosyncratic features. Structure 15:1505–1516
Braband A, Cameron SL, Podsiadlowski L, Daniels SR, Mayer G (2010) The mitochondrial genome of the onychophoran Opisthopatus cinctipes (Peripatopsidae) reflects the ancestral mitochondrial gene arrangement of Panarthropoda and Ecdysozoa. Mol Phylogenet Evol 57:285–292
Brindefalk B, Viklund J, Larsson D, Thollesson M, Andersson SG (2007) Origin and evolution of the mitochondrial aminoacyl-tRNA synthetases. Mol Biol Evol 24:743–756
Brown WM, George M, Wilson AC (1979) Rapid evolution of animal mitochondrial DNA. Proc Natl Acad Sci USA 76:1967–1971
Bullard J, Cai Y-C, Spremulli L (2000) Expression and characterization of the human mitochondrial leucyl-tRNA synthetase. Biochem Biophys Acta 1490:245–258
Cader MZ, Ren J, James PA, Bird LE, Talbot K, Stammers DK (2007) Crystal structure of human wildtype and S581L-mutant glycyl-tRNA synthetase, an enzyme underlying distal spinal muscular atrophy. FEBS Lett 581:2959–2964
Castellana S, Vicario S, Saccone C (2011) Evolutionary patterns of the mitochondrial genome in Metazoa: exploring the role of mutation and selection in mitochondrial protein coding genes. Genome Biol Evol 3:1067–1079
Chacinska A, Koehler CM, Milenkovic D, Lithgow T, Pfanner N (2009) Importing mitochondrial proteins: machineries and mechanisms. Cell 1387:628–644
Chimnaronk S, Gravers Jeppesen M, Suzuki T, Nyborg J, Watanabe K (2005) Dual-mode recognition of noncanonical tRNAs(Ser) by seryl-tRNA synthetase in mammalian mitochondria. EMBO J 24:3369–3379
de Bruijn MH, Schreier PH, Eperon IC, Barrell BG, Chen EY, Armstrong PW, Wong JF, Roe BA (1980) A mammalian mitochondrial serine transfer RNA lacking the “dihydrouridine” loop and stem. Nucleic Acids Res 8:5213–5222
Dörner M, Altmann M, Pääbo S, Mörl M (2001) Evidence for import of a lysyl-tRNA into marsupial mitochondria. Mol Biol Cell 12:2688–2698
Duchêne AM, Pujol C, Maréchal-Drouard L (2009) Import of tRNAs and aminoacyl-tRNA synthetases into mitochondria. Curr Genet 55:1–18
Edvardson S, Shaag A, Kolesnikova O, Gomori JM, Tarassov I, Einbinder T, Saada A, Elpeleg O (2007) Deleterious mutation in the mitochondrial arginyl-transfer RNA synthetase gene is associated with pontocerebellar hypoplasia. Am J Hum Genet 81:857–862
Elo JM, Yadavalli SS, Euro L, Isohanni P, Götz A, Carroll CJ, Valanne L, Alkuraya FS, Uusimaa J, Paetau A, Caruso EM, Pihko H, Ibba M, Tyynismaa H, Suomalainen A (2012) Mitochondrial phenylalanyl-tRNA synthetase mutations underlie fatal infantile Alpers encephalopathy. Hum Mol Genet 21:4521–4529
Enriquez JA, Attardi G (1996) Analysis of aminoacylation of human mitochondrial tRNAs. Methods Enzymol 264:183–196
Fender A, Gaudry A, Jühling F, Sissler M, Florentz C (2012) Adaptation of aminoacylation rules to mammalian mitochondria. Biochimie 94:1090–1097
Fender A, Sauter C, Messmer M, Pütz J, Giegé R, Florentz C, Sissler M (2006) Loss of a primordial identity element for a mammalian mitochondrial aminoacylation system. J Biol Chem 281:15980–15986
Florentz C, Sissler M (2001) Disease-related versus polymorphic mutations in human mitochondrial tRNAs: where is the difference? EMBO Rep 2(6):481–486
Florentz C, Sissler M (2003) Mitochondrial tRNA aminoacylation and human diseases. In: Lapointe J, Brakier-Gingras L (eds) Translation mechanisms. Landes Bioscience, Georgetown, pp 129–143
Florentz C, Sohm B, Tryoen-Tóth P, Pütz J, Sissler M (2003) Human mitochondrial tRNAs in health and disease. Cell Mol Life Sci 60:1356–1375
Frechin M, Duchêne A-M, Becker HD (2009a) Translating organellar glutamine codons: A case by case scenario? RNA Biol 6:31–34
Frechin M, Senger B, Brayé M, Kern D, Martin RP, Becker HD (2009b) Yeast mitochondrial Gln-tRNA(Gln) is generated by a GatFAB-mediated transamidation pathway involving Arc1p-controlled subcellular sorting of cytosolic GluRS. Genes Dev 23:1119–1130
Friederich MW, Hagerman PJ (1997) The angle between the anticodon and aminoacyl acceptor stems of yeast tRNA(Phe) is strongly modulated by magnesium ions. Biochemistry 36:6090–6099
Gaudry A, Lorber B, Messmer M, Neuenfeldt A, Sauter C, Florentz C, Sissler M (2012) Redesigned N-terminus enhances expression, solubility, and crystallisability of mitochondrial enzyme. Protein Eng Des Sel 25:473–481
Giegé R (2008) Toward a more complete view of tRNA biology. Nat Struct Mol Biol 15:1007–1014
Giegé R, Florentz C, Kern D, Gangloff J, Eriani G, Moras D (1996) Aspartate identity of transfer RNAs. Biochimie 78:605–623
Giegé R, Jühling F, Pütz J, Stadler P, Sauter C, Florentz C (2012) Structure of transfer RNAs: similarity and variability. Wiley Interdiscip Rev RNA 3:37–61
Giegé R, Sissler M, Florentz C (1998) Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res 26:5017–5035
Goto Y, Nonaka I, Horai S (1990) A mutation in the tRNALeu(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature 348:651–653
Götz A, Tyynismaa H, Euro L, Ellonen P, Hyötyläinen T, Ojala T, Hämäläinen RH, Tommiska J, Raivio T, Oresic M, Karikoski R, Tammela O, Simola KO, Paetau A, Tyni T, Suomalainen A (2011) Exome sequencing identifies mitochondrial alanyl-tRNA synthetase mutations in infantile mitochondrial cardiomyopathy. Am J Hum Genet 88:635–642
Guo M, Ignatov M, Musier-Forsyth K, Schimmel P, Yang XL (2008) Crystal structure of tetrameric form of human lysyl-tRNA synthetase: Implications for multisynthetase complex formation. Proc Natl Acad Sci USA 105:2331–2336
Guo M, Schimmel P (2013) Essential nontranslational functions of tRNA synthetases. Nat Chem Biol 9:145–153
Guo M, Schimmel P, Yang X-L (2010a) Functional expansion of human tRNA synthetases achieved by structural inventions. FEBS Lett 584:434–442
Guo M, Yang XL, Schimmel P (2010b) New functions of aminoacyl-tRNA synthetases beyond translation. Nat Rev Mol Cell Biol 11:668–674
Haen KM, Pett W, Lavrov DV (2010) Parallel loss of nuclear-encoded mitochondrial aminoacyl-tRNA synthetases and mtDNA-encoded tRNAs in Cnidaria. Mol Biol Evol 27:2216–2219
Helm M, Attardi G (2004) Nuclear control of cloverleaf structure of human mitochondrial tRNA(Lys). J Mol Biol 337:545–560
Helm M, Brulé H, Degoul F, Cepanec C, Leroux J-P, Giegé R, Florentz C (1998) The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA. Nucleic Acids Res 26:1636–1643
Helm M, Brulé H, Friede D, Giegé R, Pütz J, Florentz C (2000) Search for characteristic structural features of mammalian mitochondrial tRNAs. RNA 6:1356–1379
Helm M, Florentz C, Chomyn A, Attardi G (1999) Search for differences in post-transcriptional modification patterns of mitochondrial DNA-encoded wild-type and mutant human tRNALys and tRNALeu(UUR). Nucleic Acids Res 27:756–763
Hou YM, Yang X (2013) Regulation of cell death by transfer RNA. Antioxid Redox Signal [Epub ahead of print]
Ibba M, Francklyn C, Cusack S (2005) The aminoacyl-tRNA synthetases. Landes Biosciences, Georgetown
Jacobs HT, Holt IJ (2000) The np 3243 MELAS mutation: damned if you aminoacylate, damned if you don’t. Hum Mol Genet 1:463–465
Jacobs HT (2003) Disorders of mitochondrial protein synthesis. Hum Mol Genet 12:R293–301
Jia J, Arif A, Ray PS, Fox PL (2008) WHEP domains direct noncanonical function of glutamyl-Prolyl-tRNA synthetase in translational control of gene expression. Mol Cell 29:679–690
Jühling F, Pütz J, Bernt M, Donath A, Middendorf M, Florentz C, Stadler PF (2012a) Improved systematic tRNA gene annotation allows new insights into the evolution of mitochondrial tRNA structures and into the mechanisms of mitochondrial genome rearrangements. Nucleic Acids Res 40:2833–2845
Jühling F, Pütz J, Florentz C, Stadler PF (2012b) Armless mitochondrial tRNAs in Enoplea (Nematoda). RNA Biol 9:1161–1166
Kim DG, Choi JW, Lee JY, Kim H, Oh YS, Lee JW, Tak YK, Song JM, Razin E, Yun SH, Kim S (2012) Interaction of two translational components, lysyl-tRNA synthetase and p40/37LRP, in plasma membrane promotes laminin-dependent cell migration. FASEB J 26:4142–4159
Kirino Y, Goto Y, Campos Y, Arenas J, Suzuki T (2005) Specific correlation between the wobble modification deficiency in mutant tRNAs and the clinical features of a human mitochondrial disease. Proc Natl Acad Sci USA 102:7127–7132
Kleiman L, Cen S (2004) The tRNALys packaging complex in HIV-1. Int J Biochem Cell Biol 36:1776–1786
Klipcan L, Levin I, Kessler N, Moor N, Finarov I, Safro M (2008) The tRNA-induced conformational activation of human mitochondrial phenylalanyl-tRNA synthetase. Structure 16:1095–1104
Klipcan L, Moor N, Finarov I, Kessler N, Sukhanova M, Safro MG (2012) Crystal structure of human mitochondrial PheRS complexed with tRNA(Phe) in the active “open” state. J Mol Biol 415:527–537
Konovalova S, Tyynismaa H (2013) Mitochondrial aminoacyl-tRNA synthetases in human disease. Mol Genet Metab [Epub ahead of print]
Kumazawa Y, Himeno H, Miura K, Watanabe K (1991) Unilateral aminoacylation specificity between bovine mitochondria and eubacteria. J Biochem 109:421–427
LaRiviere FJ, Wolfson AD, Uhlenbeck OC (2001) Uniform binding of aminoacyl-tRNAs to elongation factor Tu by thermodynamic compensation. Science 294:165–168
Laslett D, Canbäck B (2008) ARWEN: a program to detect tRNA genes in metazoan mitochondrial nucleotide sequences. Bioinformatics 24:172–175
Leontis NB, Stombaugh J, Westhof E (2002) The non-Watson-Crick base pairs and their associated isostericity matrices. Nucleic Acids Res 30:3497–3531
Levinger L, Mörl M, Florentz C (2004) Mitochondrial tRNA 3′ end metabolism and human disease. Nucleic Acids Res 32:5430–5441
Lowe TM, Eddy SR (1997) tRNAscan-SE: a program for improved detection of transfer RNA genes in genomic sequence. Nucleic Acids Res 25:955–964
Macey JR, Larson A, Ananjeva NB, Papenfuss TJ (1997) Replication slippage may cause parallel evolution in the secondary structures of mitochondrial transfer RNAs. Mol Biol Evol 14:30–39
McFarland R, Elson JL, Taylor RW, Howell N, Turnbull DM (2004) Assigning pathogenicity to mitochondrial tRNA mutations: when ‘definitely maybe’ is not good enough. Trends Genet 20:591–596
Mei Y, Yong J, Liu H, Shi Y, Meinkoth J, Dreyfuss G, Yang X (2010) tRNA binds to cytochrome c and inhibits caspase activation. Mol Cell 37:688–698
Messmer M, Pütz J, Suzuki T, Suzuki T, Sauter C, Sissler M, Florentz C (2009) Tertiary network in mammalian mitochondrial tRNAAsp revealed by solution probing and phylogeny. Nucleic Acids Res 37:6881–6895
Miyamoto H, Machida RJ, Nishida S (2010) Complete mitochondrial genome sequences of the three pelagic chaetognaths Sagitta nagae, Sagitta decipiens and Sagitta enflata. Comp Biochem Physiol Part D Genomics Proteomics 5:65–72
Motorin Y, Helm M (2010) tRNA stabilization by modified nucleotides. Biochemistry 49:4934–4944
Mudge SJ, Williams JH, Eyre HJ, Sutherland GR, Cowan PJ, Power DA (1998) Complex organisation of the 5′-end of the human glycine tRNA synthetase gene. Gene 209:45–50
Nagao A, Suzuki T, Katoh T, Sakaguchi Y, Suzuki T (2009) Biogenesis of glutaminyl-mt tRNAGln in human mitochondria. Proc Natl Acad Sci USA 106:16209–16214
Nagao A, Suzuki T, Suzuki T (2007) Aminoacyl-tRNA surveillance by EF-Tu in mammalian mitochondria. Nucleic Acids Symp Ser (Oxf) 51:41–42
Nawroki EP, Kolbe DL, Eddy SR (2009) Infernal 1.0: Inference of RNA Alignments. Bioinformatics 25:1335–1337
Neuenfeldt A, Lorber B, Ennifar E, Gaudry A, Sauter C, Sissler M, Florentz C (2013) Thermodynamic properties distinguish human mitochondrial aspartyl-tRNA synthetase from bacterial homolog with same 3D architecture. Nucleic Acids Res 41:2698–2708
Ofir-Birin Y, Fang P, Bennett SP, Zhang HM, Wang J, Rachmin I, Shapiro R, Song J, Dagan A, Pozo J, Kim S, Marshall AG, Schimmel P, Yang XL, Nechushtan H, Razin E, Guo M (2013) Structural switch of lysyl-tRNA synthetase between translation and transcription. Mol Cell 49:30–42
Park MC, Kang T, Jin D, Han JM, Kim SB, Park YJ, Cho K, Park YW, Guo M, He W, Yang XL, Schimmel P, Kim S (2012) Secreted human glycyl-tRNA synthetase implicated in defense against ERK-activated tumorigenesis. Proc Natl Acad Sci USA 109:E640–E647
Park SG, Schimmel P, Kim S (2008) Aminoacyl tRNA synthetases and their connections to disease. Proc Natl Acad Sci USA 105:11043–11049
Pierce SB, Chisholm KM, Lynch ED, Lee MK, Walsh T, Opitz JM, Li W, Klevit RE, King MC (2011) Mutations in mitochondrial histidyl tRNA synthetase HARS2 cause ovarian dysgenesis and sensorineural hearing loss of Perrault syndrome. Proc Natl Acad Sci USA 108:6543–6548
Pruitt KD, Tatusova T, Maglott DR (2007) NCBI reference sequences (RefSeq): a curated non-redundant sequence database of genomes, transcripts and proteins. Nucleic Acids Res 5(Database issue):D61–D65
Pütz J, Dupuis B, Sissler M, Florentz C (2007) Mamit-tRNA, a database of mammalian mitochondrial tRNA primary and secondary structures. RNA 13:1184–1190
Riley LG, Cooper S, Hickey P, Rudinger-Thirion J, McKenzie M, Compton A, Lim SC, Thorburn D, Ryan MT, Giegé R, Bahlo M, Christodoulou J (2010) Mutation of the mitochondrial tyrosyl-tRNA synthetase gene, YARS2, causes myopathy, lactic acidosis, and sideroblastic anemia–MLASA syndrome. Am J Hum Genet 87:52–59
Rinehart J, Krett B, Rubio M-AT, Alfonzo JD, Söll D (2005) Saccharomyces cerevisiae imports the cytosolic pathway for Gln-tRNA synthesis into the mitochondion. Genes Dev 19:583–592
Rötig A (2011) Human diseases with impaired mitochondrial protein synthesis. Biochim Biophys Acta 1807:1198–1205
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, Krageloh-Mann I, Smeitink JA, Florentz C, Coster RV, Pronk JC, van der Knaap MS (2007) Mitochondrial aspartyl-tRNA synthetase deficiency causes leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation. Nat Genet 39:534–539
Schwenzer H, Zoll J, Florentz C, Sissler M (2013) Pathogenic implications of human mitochondrial aminoacyl-tRNA synthetases. In: KIM (ed) Topics in current chemistry-aminoacyl-tRNA synthetases: Applications in chemistry, Biology and Medicine. Springer (in press)
Segovia R, Pett W, Trewick S, Lavrov DV (2011) Extensive and evolutionarily persistent mitochondrial tRNA editing in Velvet Worms (phylum Onychophora). Mol Biol Evol 28:2873–2881
Seutin G, Lang BF, Mindell DP, Morais R (1994) Evolution of the WANCY region in amniote mitochondrial DNA. Mol Biol Evol 11:329–340
Shiba K, Schimmel P, Motegi H, Noda T (1994) Human glycyl-tRNA synthetase. Wide divergence of primary structure from bacterial counterpart and species-specific aminoacylation. J Biol Chem 269:30049–30055
Shoffner J, Lott M, Lezza AMS, Seibel P, Ballinger SW, Wallace DC (1990) Myoclonic epilepsy and ragged red fiber disease (MERRF) is associated with mitochondrial DNA tRNALys mutation. Cell 61:931–937
Sissler M, Pütz J, Fasiolo F, Florentz C (2005) Mitochondrial aminoacyl-tRNA synthetases. In: Ibba M, Francklyn C, Cusack S (eds), Aminoacyl-tRNA synthetases, chapter 24, pp 271–284. Landes Biosciences, Georgetown
Sohm B, Frugier M, Brulé H, Olszak K, Przykorska A, Florentz C (2003) Towards understanding human mitochondrial leucine aminoacylation identity. J Mol Biol 328:995–1010
Steenweg ME, Ghezzi D, Haack T, Abbink TE, Martinelli D, van Berkel CG, Bley A, Diogo L, Grillo E, Te Water Naudé J, Strom TM, Bertini E, Prokisch H, van der Knaap MS, Zeviani M (2012) Leukoencephalopathy with thalamus and brainstem involvement and high lactate ‘LTBL’ caused by EARS2 mutations. Brain 135:1387–1394
Suga K, Mark Welch DB, Tanaka Y, Sakakura Y, Hagiwara A (2008) Two circular chromosomes of unequal copy number make up the mitochondrial genome of the rotifer Brachionus plicatilis. Mol Biol Evol 25:1129–1137
Suzuki T, Nagao A, Suzuki T (2011) Human mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases. Annu Rev Genet 45:299–329
Taylor RW, Turnbull DM (2005) Mitochondrial DNA mutations in human disease. Nat Rev Genet 6:389–402
Tolkunova E, Park H, Xia J, King MP, Davidson E (2000) The human lysyl-tRNA synthetase gene encodes both the cytoplasmic and mitochondrial enzymes by means of an unusual splicing of the primary transcript. J Biol Chem 275:35063–35069
van Berge L, Dooves S, van Berkel CG, Polder E, van der Knaap MS, Scheper GC (2012) Leukoencephalopathy with brain stem and spinal cord involvement and lactate elevation is associated with cell-type-dependent splicing of mtAspRS mRNA. Biochem J 441:955–962
van der Knaap MS, van der Voorn P, Barkhof F, Van Coster R, Krägeloh-Mann I, Feigenbaum A, Blaser S, Vles JS, Rieckmann P, Pouwels PJ (2003) A new leukoencephalopathy with brainstem and spinal cord involvement and high lactate. Ann Neurol 53:252–258
Wakasugi K, Slike BM, Hood J, Ewalt KL, Cheresh DA, Schimmel P (2002a) Induction of angiogenesis by a fragment of human tyrosyl-tRNA synthetase. J Biol Chem 277:20124–20126
Wakasugi K, Slike BM, Hood J, Otani A, Ewalt KL, Friedlander M, Cheresh DA, Schimmel P (2002b) A human aminoacyl-tRNA synthetase as a regulator of angiogenesis. Proc Natl Acad Sci USA 99:173–177
Wakita K, Watanabe Y-I, Yokogawa T, Kumazawa Y, Nakamura S, Ueda T, Watanabe K, Nishikawa K (1994) Higher-order structure of bovine mitochondrial tRNAPhe lacking the ‘conserved’ GG and TYCG sequences as inferred by enzymatic and chemical probing. Nucleic Acids Res 22:347–353
Wang X, Lavrov DV (2008) Seventeen new complete mtDNA sequences reveal extensive mitochondrial genome evolution within the Demospongiae. PLoS ONE 3:e2723
Watanabe K (2010) Unique features of animal mitochondrial translation systems. The non-universal genetic code, unusual features of the translational apparatus and their relevance to human mitochondrial diseases. Proc Jpn Acad Ser B Phys Biol Sci 86:11–36
Willkomm DK, Hartmann RK (2006) Intricacies and surprises of nuclear-mitochondrial co-evolution. Biochem J 399:e7–e9
Wittenhagen LM, Kelley SO (2003) Impact of disease-related mitochondrial mutations on tRNA structure and function. Trends Biochem Sci 28:605–611
Woese CR, Olsen GJ, Ibba M, Söll D (2000) Aminoacyl-tRNA synthetases, the genetic code, and the evolutionary process. Microbiol and Mol Biol Reviews 64:202–236
Wolstenholme DR, Okimoto R, Mcfarlane JL (1994) Nucleotide correlations that suggest tertiary interactions in the TV-replacement loop-containing mitochondrial tRNAs of the nematodes, Caenorhabditis elegans and Ascaris suum. Nucleic Acids Res 22:4300–4306
Xie W, Schimmel P, Yang XL (2006) Crystallization and preliminary X-ray analysis of a native human tRNA synthetase whose allelic variants are associated with Charcot-Marie-Tooth disease. Acta Crystallograph Sect F Struct Biol Cryst Commun 62:1243–1246
Yadavalli SS, Klipcan L, Zozulya A, Banerjee R, Svergun D, Safro M, Ibba M (2009) Large-scale movement of functional domains facilitates aminoacylation by human mitochondrial phenylalanyl-tRNA synthetase. FEBS Lett 583:3204–3208
Yao YN, Wang L, Wu XF, Wang ED (2003) The processing of human mitochondrial leucyl-tRNA synthetase in the insect cells. FEBS Lett 534:139–142
Yarham JW, Al-Dosary M, Blakely EL, Alston CL, Taylor RW, Elson JL, McFarland R (2011) A comparative analysis approach to determining the pathogenicity of mitochondrial tRNA mutations. Hum Mutat 32:1319–1325
Yarham JW, Elson JL, Blakely EL, McFarland R, Taylor RW (2010) Mitochondrial tRNA mutations and disease. Wiley Interdiscip Rev RNA 1:304–324
Ylikallio E, Suomalainen A (2012) Mechanisms of mitochondrial diseases. Ann Med 44:41–59
Acknowledgments
We thank Richard Giegé for critical reading of the manuscript and Gert Scheper and Koen de Groot for help in the qPCR experiments. Numerous contributions on mt-tRNAs and aaRS could not be mentioned because of space limitation and we apologize for this. Financial support came from Centre National de la Recherche Scientifique (CNRS), Université de Strasbourg, ANR MITOMOT (ANR-09-BLAN-0091-01/03), French National Program ‘Investissements d’Avenir’ (Labex MitoCross) administered by the “Agence National de la Recherche”, and referenced ANR-10-IDEX-002-02; French-German PROCOPE program (DAAD D/0628236, EGIDE PHC 14770PJ), and German Academic Exchange Service (DAAD D/10/43622) for a doctoral fellowship.
Author information
Authors and Affiliations
Corresponding author
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2013 Springer-Verlag Berlin Heidelberg
About this chapter
Cite this chapter
Florentz, C. et al. (2013). Translation in Mammalian Mitochondria: Order and Disorder Linked to tRNAs and Aminoacyl-tRNA Synthetases. In: Duchêne, AM. (eds) Translation in Mitochondria and Other Organelles. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-39426-3_3
Download citation
DOI: https://doi.org/10.1007/978-3-642-39426-3_3
Published:
Publisher Name: Springer, Berlin, Heidelberg
Print ISBN: 978-3-642-39425-6
Online ISBN: 978-3-642-39426-3
eBook Packages: Biomedical and Life SciencesBiomedical and Life Sciences (R0)