Taylor, RW, Turnbull, DM. Mitochondrial DNA mutations in human disease. Nat Rev Genet 2005, 6: 389–402.
Zeviani, M, Di Donato, S. Mitochondrial disorders. Brain 2004, 127: 2153–2172.
Cree, LM, Samuels, DC, Lopes, S, Rajasimha, HK, Wonnapinij, P, Mann, JR, Dahl, HHM, Chinnery, PF. A reduction of mitochondrial DNA molecules during embryogenesis explains the rapid segregation of genotypes. Nat Genet 2008, 40: 249–254.
Stewart, JB, Freyer, C, Elson, JL, Larsson, NG. Purifying selection of mtDNA and its implications for understanding evolution and mitochondrial disease. Nat Rev Genet 2008, 9: 657–662.
Wai, T, Teoli, D, Shoubridge, EA. The mitochondrial DNA genetic bottleneck results from replication of a subpopulation of genomes. Nat Genet 2008, 40: 1484–1488.
Cao, LQ, Shitara, H, Horii, T, Nagao, Y, Imai, H, Abe, K, Hara, T, Hayashi, JI, Yonekawa, H. The mitochondrial bottleneck occurs without reduction of mtDNA content in female mouse germ cells. Nat Genet 2007, 39: 386–390.
Anderson, S, Bankier, AT, Barrell, BG, Debruijn, MHL, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, Sanger, F, et al. Sequence and organisation of the human mitochondrial genome. Nature 1981, 290: 457–465.
Taanman, JW. The mitochondrial genome: structure, transcription, translation and replication. Biochim Biophys Acta 1999, 1410: 103–123.
Larsson, NG, Clayton, DA. Molecular genetic aspects of human mitochondrial disorders. Ann Rev Genet 1995, 29: 151–178.
Robin, ED, Wong, R. Mitochondrial DNA molecules and virtual number of mitochondria per cell in mammalian cells. J Cell Physiol 1988, 136: 507–513.
Ojala, D, Montoya, J, Attardi, G. Transfer‐RNA punctuation model of RNA processing in human mitochondria. Nature 1981, 290: 470–474.
Florentz, C, Sohm, B, Tryoen‐Toth, P, Putz, J, Sissler, M. Human mitochondrial tRNAs in health and disease. Cell Mol Life Sci 2003, 60: 1356–1375.
Pesole, G, Gissi, C, De Chirico, A, Saccone, C. Nucleotide substitution rate of mammalian mitochondrial genomes. J Mol Evol 1999, 48: 427–434.
Kunkel, TA, Loeb, LA. Fidelity of mammalian DNA‐polymerases. Science 1981, 213: 765–767.
Mandavilli, BS, Santos, JH, Van Houten, B. Mitochondrial DNA repair and aging. Mut Res 2002, 509: 127–151.
Durham, SE, Samuels, DC, Chinnery, PF. Is selection required for the accumulation of somatic mitochondrial DNA mutations in post‐mitotic cells? Neuromus Disord 2006, 16: 381–386.
Sacconi, S, Salviati, L, Nishigaki, Y, Walker, WF, Hernandez‐Rosa, E, Trevisson, E, Delplace, S, Desnuelle, C, Shanske, S, Hirano, M, et al. A functionally dominant mitochondrial DNA mutation. Hum Mol Genet 2008, 17: 1814–1820.
Elson, JL, Swalwell, H, Blakely, EL, McFarland, R, Taylor, RW, Turnbull, DM. Pathogenic mitochondrial tRNA mutations—which mutations are inherited and why? Hum Mutat 2009, 30: E984–E992.
Lightowlers, RN, Chinnery, PF, Turnbull, DM, Howell, N. Mammalian mitochondrial genetics: heredity, heteroplasmy and disease. Trends Genet 1997, 13: 450–455.
He, YP, Wu, J, Dressman, DC, Iacobuzio‐Donahue, C, Markowitz, SD, Velculescu, VE, Diaz, LA, Kinzler, KW, Vogelstein, B, Papadopoulos, N. Heteroplasmic mitochondrial DNA mutations in normal and tumour cells. Nature 2010, 464: 610–614.
McFarland, R, Elson, JL, Taylor, RW, Howell, N, Turnbull, DM. Assigning pathogenicity to mitochondrial tRNA mutations: when ‘definitely maybe’ is not good enough. Trends Genet 2004, 20: 591–596.
Stewart, JB, Freyer, C, Elson, JL, Wredenberg, A, Cansu, Z, Trifunovic, A, Larsson, NG. Strong purifying selection in transmission of mammalian mitochondrial DNA. PLoS Biol 2008, 6: 63–71.
Kogelnik, AM, Lott, MT, Brown, MD, Navathe, SB, Wallace, DC. MITOMAP: an update on the status of the human mitochondrial genome database. Nucleic Acids Res 1997, 25: 196–199.
Martin, NC. %22Organellar tRNAs: biosynthesis and function%22. In: Soll, D, RajBhandary, UL, eds. tRNA: Structure, Biosynthesis and Function. Washington, DC: ASM Press; 1995, 127–140.
Helm, M, Brule, H, Friede, D, Giege, R, Putz, D, Florentz, C. Search for characteristic structural features of mammalian mitochondrial tRNAs. RNA 2000, 6: 1356–1379.
Takeuchi, N, Kawakami, M, Omori, A, Ueda, T, Spremulli, LL, Watanabe, K. Mammalian mitochondrial methionyl‐tRNA transformylase from bovine liver—purification, characterization, and gene structure. J Biol Chem 1998, 273: 15085–15090.
Takeuchi, N, Vial, L, Panvert, M, Schmitt, E, Watanabe, K, Mechulam, Y, Blanquet, S. Recognition of tRNAs by methionyl‐tRNA transformylase from mammalian mitochondria. J Biol Chem 2001, 276: 20064–20068.
Spencer, AC, Spremulli, LL. Interaction of mitochondrial initiation factor 2 with mitochondrial fMet‐tRNA. Nucleic Acids Res 2004, 32: 5464–5470.
Nissen, P, Thirup, S, Kjeldgaard, M, Nyborg, J. The crystal structure of Cys‐tRNACys‐EF‐Tu‐GDPNP reveals general and specific features in the ternary complex and in tRNA. Structure 1999, 7: 143–156.
Ohtsuki, T, Sato, A, Watanabe, Y, Watanabe, K. A unique serine‐specific elongation factor Tu found in nematode mitochondria. Nat Struct Biol 2002, 9: 669–673.
Helm, M, Brule, H, Degoul, F, Cepanec, C, Leroux, JP, Giege, R, Florentz, C. The presence of modified nucleotides is required for cloverleaf folding of a human mitochondrial tRNA. Nucleic Acids Res 1998, 26: 1636–1643.
Frank, DN, Pace, NR. Ribonuclease P: unity and diversity in a tRNA processing ribozyme. Ann Rev Biochem 1998, 67: 153–180.
Manam, S, Vantuyle, GC. Separation and characterisation of 5′‐transfer and 3′‐transfer RNA processing nucleases from rat‐liver mitochondria. J Biol Chem 1987, 262: 10272–10279.
Mukerji, SK, Deutscher, MD. Reactions at 3′ terminus of transfer ribonucleic‐acid: V. Subcellular localisation and evidence for a mitochondrial transfer ribonucleic acid nucleotidyltransferase. J Biol Chem 1972, 247: 481–488.
Meinnel, T, Mechulam, Y, Blanquet, S. %22Aminoacyl‐tRNA synthetases: occurence, structure and function%22. In: Soll, D, RajBhandary, UL, eds. tRNA: Structure, Biosynthesis and Function. Washington, DC: ASM Press; 1995, 251–292.
Sissler, M, Putz, J, Fasiolo, F, Florentz, C. %22Mitochondrial aminoacyl‐tRNA synthetases%22. In: Ibba, M, Francklyn, C, Cusack, S, eds. The Aminoacyl‐tRNA Synthetases. Georgetown, TX: Landes Biosciences; 2005.
Sasarman, F, Antonicka, H, Shoubridge, EA. The A3243G tRNALeu(UUR) MELAS mutation causes amino acid misincorporation and a combined respiratory chain assembly defect partially suppressed by overexpression of EFTu and EFG2. Hum Mol Genet 2008, 17: 3697–3707.
Boniecki, MT, Vu, MT, Betha, AK, Martinis, SA. CP1‐dependent partitioning of pretransfer and posttransfer editing in leucyl‐tRNA synthetase. Proc Natl Acad Sci USA 2008, 105: 19223–19228.
Karkhanis, VA, Boniecki, MT, Poruri, K, Martinis, SA. A viable amino acid editing activity in the leucyl‐tRNA synthetase CP1‐splicing domain is not required in the yeast mitochondria. J Biol Chem 2006, 281: 33217–33225.
Lue, SW, Kelley, SO. An aminoacyl‐tRNA synthetase with a defunct editing site. Biochemistry 2005, 44: 3010–3016.
Roy, H, Ling, JQ, Alfonzo, J, Ibba, M. Loss of editing activity during the evolution of mitochondrial phenylalanyl‐tRNA synthetase. J Biol Chem 2005, 280: 38186–38192.
Yamane, T, Hopfield, JJ. Experimental evidence for kinetic proofreading in aminoacylation of transfer‐RNA by synthetase. Proc Natl Acad Sci USA 1977, 74: 2246–2250.
Giege, R, Sissler, M, Florentz, C. Universal rules and idiosyncratic features in tRNA identity. Nucleic Acids Res 1998, 26: 5017–5035.
Barrell, BG, Anderson, S, Bankier, AT, Debruijn, MHL, Chen, E, Coulson, AR, Drouin, J, Eperon, IC, Nierlich, DP, Roe, BA, et al. Different pattern of codon recognition by mammalian mitochondrial transfer‐RNAs. Proc Natl Acad Sci USA 1980, 77: 3164–3166.
Barrell, BG, Bankier, AT, Drouin, J. Different genetic‐code in human mitochondria. Nature 1979, 282: 189–194.
Lander, ES, Linton, LM, Birren, B, Nusbaum, C, Zody, MC, Baldwin, J, Devon, K, Dewar, K, Doyle, M, FitzHugh, W, et al. Initial sequencing and analysis of the human genome. Nature 2001, 409: 860–921.
Crick, FH. Codon–anticodon pairing: the wobble hypothesis. J Mol Biol 1966, 19: 548–555.
Yasukawa, T, Suzuki, T, Ishii, N, Ueda, T, Ohta, S, Watanabe, K. Defect in modification at the anticodon wobble nucleotide of mitochondrial tRNALys with the MERRF encephalomyopathy pathogenic mutation. FEBS Lett 2000, 467: 175–178.
Yasukawa, T, Suzuki, T, Ueda, T, Ohta, S, Watanabe, K. Modification defect at anticodon wobble nucleotide of mitochondrial tRNAsLeu(UUR) with pathogenic mutations of mitochondrial myopathy, encephalopathy, lactic acidosis, and stroke‐like episodes. J Biol Chem 2000, 275: 4251–4257.
Manwaring, N, Jones, MM, Wang, JJ, Rochtchina, E, Howard, C, Mitchell, P, Sue, CM. Population prevalence of the MELAS A3243G mutation. Mitochondrion 2007, 7: 230–233.
Majamaa, K, Moilanen, JS, Uimonen, S, Remes, AM, Salmela, PI, Karppa, M, Majamaa‐Voltti, KAM, Rusanen, H, Sorri, M, Peuhkurinen, KJ, et al. Epidemiology of A3243G, the mutation for mitochondrial encephalomyopathy, lactic acidosis, and strokelike episodes: prevalence of the mutation in an adult population. Am J Hum Genet 1998, 63: 447–454.
Schaefer, AM, McFarland, R, Blakely, EL, He, L, Whittaker, RG, Taylor, RW, Chinnery, PF, Turnbull, DM. Prevalence of mitochondrial DNA disease in adults. Ann Neurol 2008, 63: 35–39.
Dimauro, S, Schon, EA. Mitochondrial DNA mutations in human disease. Am J Med Genet 2001, 106: 18–26.
Deschauer, M, Swalwell, H, Strauss, M, Zierz, S, Taylor, RW. Novel mitochondrial transfer RNAPhe gene mutation associated with late‐onset neuromuscular disease. Arch Neurol 2006, 63: 902–905.
Mimaki, M, Hatakeyama, H, Ichiyama, T, Isumi, H, Furukawa, S, Akasaka, M, Kamei, A, Komaki, H, Nishino, I, Nonaka, I, et al. Different effects of novel mtDNA G3242A and G3244A base changes adjacent to a common A3243G mutation in patients with mitochondrial disorders. Mitochondrion 2009, 9: 115–122.
Bortot, B, Barbi, E, Biffi, S, Angelini, C, Faleschini, E, Severini, GM, Carrozzi, M. Two novel cosegregating mutations in tRNAMet and COX III, in a patient with exercise intolerance and autoimmune polyendocrinopathy. Mitochondrion 2009, 9: 123–129.
Sanaker, PS, Nakkestad, HL, Downham, E, Bindoff, LA. A novel mutation in the mitochondrial tRNA for tryptophan causing a late‐onset mitochondrial encephalomyopathy. Acta Neurol Scand 2010, 121: 109–113.
Swalwell, H, Deschauer, M, Hartl, H, Strauss, M, Turnbull, DM, Zierz, S, Taylor, RW. Pure myopathy associated with a novel mitochondrial tRNA gene mutation. Neurology 2006, 66: 447–449.
Meulemans, A, De Paepe, B, De Bleecker, J, Smet, J, Lissens, W, Van Coster, R, De Meirleir, L, Seneca, S. Two novel mitochondrial DNA mutations in muscle tissue of a patient with limb‐girdle myopathy. Arch Neurol 2007, 64: 1339–1343.
Smits, P, Mattijssen, S, Morava, E, van den Brand, M, van den Brandt, F, Wijburg, F, Pruijn, G, Smeitink, J, Nijtmans, L, Rodenburg, R, et al. Functional consequences of mitochondrial tRNATrp and tRNAArg mutations causing combined OXPHOS defects. Euro J Hum Genet 2010, 18: 324–329.
Kornblum, C, Zsurka, G, Wiesner, RJ, Schroder, R, Kunz, WS. Concerted action of two novel tRNA mtDNA point mutations in chronic progressive external ophthalmoplegia. Biosci Rep 2008, 28: 89–96.
Gambello, MJ, Bai, RK, Chen, TJ, Dimachkie, M, Wong, LJC. Exercise intolerance associated with a novel 8300T %3E C mutation in mitochondrial transfer RNALys. Muscle Nerve 2006, 34: 437–443.
Blakely, EL, Swalwell, H, Petty, RKH, McFarland, R, Turnbull, DM, Taylor, RW. Sporadic myopathy and exercise intolerance associated with the mitochondrial 8328G %3E A tRNALys mutation. J Neurol 2007, 254: 1283–1285.
Pereira, C, Nogueira, C, Barbot, C, Tessa, A, Soares, C, Fattori, F, Guimaraes, A, Santorelli, FM, Vilarinho, L. Identification of a new mtDNA mutation (14724G %3E A) associated with mitochondrial leukoencephalopathy. Biochem Biophys Res Commun 2007, 354: 937–941.
Blakely, EL, Trip, SA, Swalwell, H, He, LP, Wren, DR, Rich, P, Turnbull, DM, Omer, SE, Taylor, RW. A new mitochondrial transfer RNAPro gene mutation associated with myoclonic epilepsy with ragged‐red fibers and other neurological features. Arch Neurol 2009, 66: 399–402.
King, MP, Attardi, G. Human cells lacking mtDNA—repopulation with exogenous mitochondria by complementation. Science 1989, 246: 500–503.
Pakendorf, B, Stoneking, M. Mitochondrial DNA and human evolution. Ann Rev Genomics Hum Genet 2005, 6: 165–183.
Neiman, M, Taylor, DR. The causes of mutation accumulation in mitochondrial genomes. Proc R Soc B‐Biol Sci 2009, 276: 1201–1209.
D`Aurelio, M, Gajewski, CD, Lin, MT, Mauck, WM, Shao, LZ, Lenaz, G, Moraes, CT, Manfredi, G. Heterologous mitochondrial DNA recombination in human cells. Hum Mol Genet 2004, 13: 3171–3179.
Zsurka, G, Hampel, KG, Kudina, T, Kornblum, C, Kraytsberg, Y, Elger, CE, Khrapko, K, Kunz, WS. Inheritance of mitochondrial DNA recombinants in double‐heteroplasmic families: potential implications for phylogenetic analysis. Am J Hum Genet 2007, 80: 298–305.
Cann, RL, Wilson, AC. Models of Human Evolution. Science 1982, 217: 303–304.
Ingman, M, Kaessmann, H, Paabo, S, Gyllensten, U. Mitochondrial genome variation and the origin of modern humans. Nature 2000, 408: 708–713.
Elliott, HR, Samuels, DC, Eden, JA, Relton, CL, Chinnery, PF. Pathogenic mitochondrial DNA mutations are common in the general population. Am J Hum Genet 2008, 83: 254–260.
Muller, HJ. The relation of recombination to mutational advance. Mutat Res 1964, 106: 2–9.
Hauswirth, WW, Laipis, PJ. Mitochondrial DNA polymorphism in a maternal lineage of Holstein Cows. Proc Natl Acad Sci USA 1982, 79: 4686–4690.
Jenuth, JP, Peterson, AC, Fu, K, Shoubridge, EA. Random genetic drift in the female germline explains the rapid segregation of mammalian mitochondrial DNA. Nat Genet 1996, 14: 146–151.
Cao, L, Shitara, H, Sugimoto, M, Hayashi, J‐I, Abe, K, Yonekawa, H. New evidence confirms that the mitochondrial bottleneck is generated without reduction of mitochondrial DNA content in early primordial germ cells of mice. PLoS Genet 2009, 5: e1000756.
Fan, WW, Waymire, KG, Narula, N, Li, P, Rocher, C, Coskun, PE, Vannan, MA, Narula, J, MacGregor, GR, Wallace,, DC. A mouse model of mitochondrial disease reveals germline selection against severe mtDNA mutations. Science 2008, 319: 958–962.
Shoubridge, EA, Wai, T. Medicine—sidestepping mutational meltdown. Science 2008, 319: 914–915.
Elson, JL, Turnbull, DM, Howell, N. Comparative genomics and the evolution of human mitochondrial DNA: assessing the effects of selection. Am J Hum Genet 2004, 74: 229–238.
Kivisild, T, Shen, PD, Wall, DP, Do, B, Sung, R, Davis, K, Passarino, G, Underhill, PA, Scharfe, C, Torroni, A, et al. The role of selection in the evolution of human mitochondrial genomes. Genetics 2006, 172: 373–387.
Howell, N, Howell, C, Elson, JL. Time dependency of molecular rate estimates for mtDNA: this is not the time for wishful thinking. Heredity 2008, 101: 107–108.
Elson, JL, Herrnstadt, C, Preston, G, Thal, L, Morris, CM, Edwardson, JA, Beal, MF, Turnbull, DM, Howell, N. Does the mitochondrial genome play a role in the etiology of Alzheimer`s disease? Hum Genet 2006, 119: 241–254.
Finnila, S, Lehtonen, MS, Majamaa, K. Phylogenetic network for European mtDNA. Am J Hum Genet 2001, 68: 1475–1484.
Zifa, E, Giannouli, S, Theotokis, P, Stamatis, O, Mamuris, Z, Stathopoulos, C. Mitochondrial tRNA mutations—clinical and functional perturbations. RNA Biol 2007, 4: 38–66.
Pancrudo, J, Shanske, S, Coku, J, Lu, J, Mardach, R, Akman, O, Krishna, S, Bonilla, E, DiMauro, S. Mitochondrial myopathy associated with a novel mutation in mtDNA. Neuromusc Disord 2007, 17: 651–654.
Uusimaa, J, Finnila, S, Remes, AM, Rantala, H, Vainionpaa, L, Hassinen, IE, Majamaa, K. Molecular epidemiology of childhood mitochondrial encephalomyopathies in a Finnish population: sequence analysis of entire mtDNA of 17 children reveals heteroplasmic mutations in tRNAArg, tRNAGlu, and tRNALeu(UUR) genes. Pediatrics 2004, 114: 443–450.
Shoffner, JM, Lott, MT, Lezza, AMS, Seibel, P, Ballinger, SW, Wallace, DC. Myoclonic epilepsy and ragged‐red fiber disease (MERRF) is associated with a mitochondrial DNA transfer RNALys mutation. Cell 1990, 61: 931–937.
Chomyn, A, Meola, G, Bresolin, N, Lai, ST, Scarlato, G, Attardi, G. In vitro genetic transfer of protein synthesis and respiration defects to mitochondrial DNA‐less cells with myopathy‐patient mitochondria. Mol Cell Biol 1991, 11: 2236–2244.
Masucci, JP, Davidson, M, Koga, Y, Schon, EA, King, MP. In vitro analysis of mutations causing myoclonus epilepsy with ragged‐red fibers in the mitochondrial tRNALys gene—2 genotypes produce similar phenotypes. Mol Cell Biol 1995, 15: 2872–2881.
King, MP, Attardi, G. Posttranscriptional regulation of the steady‐state levels of mitochondrial transfer‐RNAs in HELA‐cells. J Biol Chem 1993, 268: 10228–10237.
Enriquez, JA, Chomyn, A, Attardi, G. mtDNA mutation in MERRF‐syndrome causes defective aminoacylation of tRNALys and premature translation termination. Nat Genet 1995, 10: 47–55.
Borner, GV, Zeviani, M, Tiranti, V, Carrara, F, Hoffmann, S, Gerbitz, KD, Lochmuller, H, Pongratz, D, Klopstock, T, Melberg, A, et al. Decreased aminoacylation of mutant tRNAs in MELAS but not in MERRF patients. Hum Mol Genet 2000, 9: 467–475.
Yasukawa, T, Suzuki, T, Ishii, N, Ohta, S, Watanabe, K. Wobble modification defect in tRNA disturbs codon–anticodon interaction in a mitochondrial disease. EMBO J 2001, 20: 4794–4802.
Yasukawa, T, Suzuki, T, Ohta, S, Watanabe, K. Wobble modification defect suppresses translational activity of tRNAs with MERRF and MELAS mutations. Mitochondrion 2002, 2: 129–141.
Ozawa, M, Nishino, I, Horai, S, Nonaka, I, Goto, Y. Myoclonus epilepsy associated with ragged‐red fibers: a G‐to‐A mutation at nucleotide pair 8363 in mitochondrial tRNALys in two families. Muscle Nerve 1997, 20: 271–278.
Goto, Y, Nonaka, I, Horai, S. A mutation in the transfer RNALeu(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies. Nature 1990, 348: 651–653.
Hammans, SR, Sweeney, MG, Brockington, M, Lennox, GG, Lawton, NF, Kennedy, CR, Morganhughes, JA, Harding, AE. The mitochondrial‐DNA transfer RNALys A‐G(8344) mutation and the syndrome of myoclonic epilepsy with ragged‐red fibers (MERRF)—relationship of clinical phenotype to proportion of mutant mitochondrial DNA. Brain 1993, 116: 617–632.
Vandenouweland, JMW, Lemkes, H, Trembath, RC, Ross, R, Velho, G, Cohen, D, Froguel, P, Maassen, JA. Maternally inherited diabetes and deafness is a distinct subtype of diabetes and associates with a single point mutation in the mitochondrial tRNALeu(UUR) gene. Diabetes 1994, 43: 746–751.
Chomyn, A, Martinuzzi, A, Yoneda, M, Daga, A, Hurko, O, Johns, D, Lai, ST, Nonaka, I, Angelini, C, Attardi, G. MELAS mutation in mtDNA binding‐site for transcription termination factor causes defects in protein‐synthesis and in respiration but no change in levels of upstream and downstream mature transcripts. Proc Natl Acad Sci U S A 1992, 89: 4221–4225.
King, MP, Koga, Y, Davidson, M, Schon, EA. Defects in mitochondrial protein‐synthesis and respiratory‐chain activity segregate with the transfer RNALeu(UUR) mutation associated with mitochondrial myopathy, encephalopathy, lactic‐acidosis, and stroke‐like episodes. Mol Cell Biol 1992, 12: 480–490.
Koga, Y, Davidson, M, Schon, EA, King, MP. Fine mapping of mitochondrial RNAs derived from the mtDNA region containing a point mutation associated with MELAS. Nucleic Acids Res 1993, 21: 657–662.
Kirino, Y, Yasukawa, T, Marjavaara, SK, Jacobs, HT, Holt, IJ, Watanabe, K, Suzuki, T. Acquisition of the wobble modification in mitochondrial tRNALeu(CUN) bearing the G12300A mutation suppresses the MELAS molecular defect. Hum Mol Genet 2006, 15: 897–904.
Wittenhagen, LM, Kelley, SO. Dimerization of a pathogenic human mitochondrial tRNA. Nat Struct Biolgy 2002, 9: 586–590.
Chinnery, PF, Howell, N, Lightowlers, RN, Turnbull, DM. Molecular pathology of MELAS and MERRF—the relationship between mutation load and clinical phenotypes. Brain 1997, 120: 1713–1721.
Chinnery, PE, Howell, N, Lightowlers, RN, Turnbull, DM. MELAS and MERRF—the relationship between maternal mutation load and the frequency of clinically affected offspring. Brain 1998, 121: 1889–1894.
Chinnery, PF, Turnbull, DM. Mitochondrial genotype and clinical phenotype. J Inherit Metab Dis 1998, 21: 321–325.
Moraes, CT, Ciacci, F, Bonilla, E, Ionasescu, V, Schon, EA, Dimauro, S. A mitochondrial transfer‐RNA anticodon swap associated with a muscle disease. Nat Genet 1993, 4: 284–288.
Brule, H, Holmes, WM, Keith, G, Giege, R, Florentz, C. Effect of a mutation in the anticodon of human mitochondrial tRNAPro on its post‐transcriptional modification pattern. Nucleic Acids Res 1998, 26: 537–543.
Taylor, RW, Giordano, C, Davidson, MM, d`Amati, G, Bain, H, Hayes, CM, Leonard, H, Barron, MJ, Casali, C, Santorelli, FM, et al. A homoplasmic mitochondrial transfer ribonucleic acid mutation as a cause of maternally inherited hypertrophic cardiomyopathy. J Am Coll Cardiol 2003, 41: 1786–1796.
Carelli, V, Giordano, C, d`Amati, G. Pathogenic expression of homoplasmic mtDNA mutations needs a complex nuclear‐mitochondrial interaction. Trends Genet 2003, 19: 257–262.
Mollers, M, Maniura‐Weber, K, Kiseljakovic, E, Bust, M, Hayrapetyan, A, Jaksch, M, Helm, M, Wiesner, RJ, von Kleist‐Retzow, JC. A new mechanism for mtDNA pathogenesis: impairment of post‐transcriptional maturation leads to severe depletion of mitochondrial tRNASer(UCN) caused by T7512C and G7497A point mutations. Nucleic Acids Res 2005, 33: 5647–5658.
Hutchin, TP, Cortopassi, GA. Mitochondrial defects and hearing loss. Cell Mol Life Sci 2000, 57: 1927–1937.
Hyslop, SJ, James, AM, Maw, M, Fischel‐Ghodsian, N, Murphy, MP. The effect on mitochondrial function of the tRNASer(UCN)/COI A7445G mtDNA point mutation associated with maternally‐inherited sensorineural deafness. Biochem Mol Biol Int 1997, 42: 567–575.
Reid, FM, Vernham, GA, Jacobs, HT. A novel mitochondrial point mutation in a maternal pedigree with sensorineural deafness. Hum Mutat 1994, 3: 243–247.
Sevior, KB, Hatamochi, A, Stewart, IA, Bykhovskaya, Y, Allen‐Powell, DR, Fischel‐Ghodsian, N, Maw, MA. Mitochondrial A7445G mutation in two pedigrees with palmoplantar keratoderma and deafness. Am J Med Genet 1998, 75: 179–185.
Chen, J, Yuan, H, Lu, J, Liu, X, Wang, G, Zhu, Y, Cheng, J, Wang, X, Han, B, Yang, L, et al. Mutations at position 7445 in the precursor of mitochondrial tRNASer(UCN) gene in three maternal Chinese pedigrees with sensorineural hearing loss. Mitochondrion 2008, 8: 285–292.
Jin, L, Yang, A, Zhu, Y, Zhao, J, Wang, X, Yang, L, Sun, D, Tao, Z, Tsushima, A, Wu, G, et al. Mitochondrial tRNASer(UCN) gene is the hot spot for mutations associated with aminoglycoside‐induced and non‐syndromic hearing loss. Biochem Biophys Res Commun 2007, 361: 133–139.
Pandya, A, Xia, X‐J, Erdenetungalag, R, Amendola, M, Landa, B, Radnaabazar, J, Dangaasuren, B, Van Tuyle, G, Nance, WE. Heterogenous point mutations in the mitochondrial tRNASer(UCN) precursor coexisting with the A1555G mutation in deaf students from Mongolia. Am J Hum Genet 1999, 65: 1803–1806.
Guan, MX, Enriquez, JA, Fischel‐Ghodsian, N, Puranam, RS, Lin, CP, Maw, MA, Attardi, G. The deafness‐associated mitochondrial DNA mutation at position 7445, which affects tRNASer(UCN) precursor processing, has long‐range effects on NADH dehydrogenase subunit ND6 gene expression. Mol Cell Biol 1998, 18: 5868–5879.
Montanari, A, Besagni, C, De Luca, C, Morea, V, Oliva, R, Tramontano, A, Bolotin‐Fukuhara, M, Frontali, L, Francisci, S. Yeast as a model of human mitochondrial tRNA base substitutions: Investigation of the molecular basis of respiratory defects. RNA 2008, 14: 275–283.
De Luca, C, Zhou, YF, Montanari, A, Morea, V, Oliva, R, Besagni, C, Bolotin‐Fukuhara, M, Frontali, L, Francisci, S. Can yeast be used to study mitochondrial diseases? Biolistic tRNA mutants for the analysis of mechanisms and suppressors. Mitochondrion 2009, 9: 408–417.
Fox, TD, Folley, LS, Mulero, JJ, McMullin, TW, Thorsness, PE, Hedin, LO, Costanzo, MC. Analysis and manipulation of yeast mitochondrial genes. Methods Enzymol 1991, 194: 149–165.
Rohou, H, Francisci, S, Rinaldi, T, Frontali, L, Bolotin‐Fukuhara, M. Reintroduction of a characterized Mit tRNA glycine mutation into yeast mitochondria provides a new tool for the study of human neurodegenerative diseases. Yeast 2001, 18: 219–227.
Park, H, Davidson, E, King, MP. Overexpressed mitochondrial leucyl‐tRNA synthetase suppresses the A3243G mutation in the mitochondrial tRNALeu(UUR) gene. RNA 2008, 14: 2407–2416.
Wallace, DC. Mitochondrial diseases in man and mouse. Science 1999, 283: 1482–1488.
Pinkert, CA, Irwin, MH, Johnson, LW, Moffatt, RJ. Mitochondria transfer into mouse ova by microinjection. Transgenic Res 1997, 6: 379–383.
Levy, SE, Waymire, KG, Kim, YL, MacGregor, GR, Wallace, DC. Transfer of chloramphenicol‐resistant mitochondrial DNA into the chimeric mouse. Transgenic Res 1999, 8: 137–145.
Inoue, K, Nakada, K, Ogura, A, Isobe, K, Goto, Y, Nonaka, I, Hayashi, JI. Generation of mice with mitochondrial dysfunction by introducing mouse mtDNA carrying a deletion into zygotes. Nat Genet 2000, 26: 176–181.
Acin‐Perez, R, Salazar, E, Brosel, S, Yang, H, Schon, EA, Manfredi, G. Modulation of mitochondrial protein phosphorylation by soluble adenylyl cyclase ameliorates cytochrome oxidase defects. EMBO Mol Med 2009, 1: 392–406.
Taivassalo, T, Fu, K, Johns, T, Arnold, D, Karpati, G, Shoubridge, EA. Gene shifting: a novel therapy for mitochondrial myopathy. Hum Mol Genet 1999, 8: 1047–1052.
Taivassalo, T, Shoubridge, EA, Chen, J, Kennaway, NG, DiMauro, S, Arnold, DL, Haller, RG. Aerobic conditioning in patients with mitochondrial myopathies: physiological, biochemical, and genetic effects. Ann Neurol 2001, 50: 133–141.
Guy, J, Qi, XP, Pallotti, F, Schon, EA, Manfredi, G, Carelli, V, Martinuzzi, A, Hauswirth, WW, Lewin, AS. Rescue of a mitochondrial deficiency causing Leber hereditary optic neuropathy. Ann Neurol 2002, 52: 534–542.
Manfredi, G, Fu, J, Ojaimi, J, Sadlock, JE, Kwong, JQ, Guy, J, Schon, EA. Rescue of a deficiency in ATP synthesis by transfer of MTATP6, a mitochondrial DNA‐encoded gene, to the nucleus. Nat Genet 2002, 30: 394–399.
Wenz, T, Diaz, F, Spiegelman, BM, Moraes, CT. Activation of the PPAR/PGC‐1 alpha pathway prevents a bioenergetic deficit and effectively improves a mitochondrial myopathy phenotype. Cell Metab 2008, 8: 249–256.
Kolesnikova, OA, Entelis, NS, Mireau, H, Fox, TD, Martin, RP, Tarassov, IA. Suppression of mutations in mitochondrial DNA by tRNAs imported from the cytoplasm. Science 2000, 289: 1931–1933.
Kamenski, P, Smirnova, E, Kolesnikova, OA, Krasheninnikov, IA, Martin, RP, Entelis, N, Tarassov, I. tRNA mitochondrial import in yeast: mapping of the import determinants in the carrier protein, the precursor of mitochondrial lysyl‐tRNA synthetase. Mitochondrion 2010, 10: 284–293.
De Luca, C, Besagni, C, Frontali, L, Bolotin‐Fukuhara, M, Francisci, S. Mutations in yeast mt tRNAs: Specific and general suppression by nuclear encoded tRNA interactors. Gene 2006, 377: 169–176.
Feuermann, M, Francisci, S, Rinaldi, T, De Luca, C, Rohou, H, Frontali, L, Bolotin‐Fukuhara, M. The yeast counterparts of human ‘MELAS’ mutations cause mitochondrial dysfunction that can be rescued by overexpression of the mitochondrial translation factor EF‐Tu. EMBO Rep 2003, 4: 53–58.
Sohm, B, Frugier, M, Brule, H, Olszak, K, Przykorska, A, Florentz, C. Towards understanding human mitochondrial leucine aminoacylation identity. J Mol Biol 2003, 328: 995–1010.
McFarland, R, Clark, KM, Morris, AAM, Taylor, RW, Macphail, S, Lightowlers, RN, Turnbull, DM. Multiple neonatal deaths due to a homoplasmic mitochondrial DNA mutation. Nat Genet 2002, 30: 145–146.
Rorbach, J, Yusoff, AA, Tuppen, H, Abg‐Kamaludin, DP, Chrzanowska‐Lightowlers, ZMA, Taylor, RW, Turnbull, DM, McFarland, R, Lightowlers, RN. Overexpression of human mitochondrial valyl tRNA synthetase can partially restore levels of cognate mt‐tRNAVal carrying the pathogenic C25U mutation. Nucleic Acids Res 2008, 36: 3065–3074.
Putz, J, Dupuis, B, Sissler, M, Florentz, C. Mamit‐tRNA, a database of mammalian mitochondrial tRNA primary and secondary structures. RNA 2007, 13: 1184–1190.
McLaren, A, Lawson, KA. How is the mouse germ‐cell lineage established? Differentiation 2005, 73: 435–437.
Temperley, R, Richter, R, Dennerlein, S, Lightowlers, RN, Chrzanowska‐Lightowlers, ZM. Hungry Codons Promote Frameshifting in Human Mitochondrial Ribosomes. Science 2010, 327: 301.