Cited by 1,635Mitochondrial Function and PathologyRNA and protein synthesis mechanismsATP Synthase and ATPases Research

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The mitochondrial genome: structure, transcription, translation and replication

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Taanman, Jan-Willem·1999·Biochimica et Biophysica Acta (BBA) - Bioenergetics

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Abstract

Mitochondria play a central role in cellular energy provision. The organelles contain their own genome with a modified genetic code. The mammalian mitochondrial genome is transmitted exclusively through the female germ line. The human mitochondrial DNA (mtDNA) is a double-stranded, circular molecule of 16569 bp and contains 37 genes coding for two rRNAs, 22 tRNAs and 13 polypeptides. The mtDNA-encoded polypeptides are all subunits of enzyme complexes of the oxidative phosphorylation system. Mitochondria are not self-supporting entities but rely heavily for their functions on imported nuclear gene products. The basic mechanisms of mitochondrial gene expression have been solved. Cis-acting mtDNA sequences have been characterised by sequence comparisons, mapping studies and mutation analysis both in vitro and in patients harbouring mtDNA mutations. Characterisation of trans-acting factors has proven more difficult but several key enzymes involved in mtDNA replication, transcription and protein synthesis have now been biochemically identified and some have been cloned. These studies revealed that, although some factors may have an additional function elsewhere in the cell, most are unique to mitochondria. It is expected that cell cultures of patients with mitochondrial diseases will increasingly be used to address fundamental questions about mtDNA expression.

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Sequence and organization of the human mitochondrial genome
Anderson, S., Bankier, A. T., Barrell, B. G., de Bruijn, M. H. L., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., Sanger, F., et al. (1981) · Nature · doi:10.1038/290457a0 · Cited by 9,740
tRNA punctuation model of RNA processing in human mitochondria
Ojala, D., Montoya, J., & Attardi, G. M. (1981) · Nature · doi:10.1038/290470a0 · Cited by 2,561
A mutation in the tRNALeu(UUR) gene associated with the MELAS subgroup of mitochondrial encephalomyopathies
Goto, Y.-I., Nonaka, I., & Horai, S. (1990) · Nature · doi:10.1038/348651a0 · Cited by 2,070
DNA TOPOISOMERASES
Wang, J. C. (1996) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.65.070196.003223 · Cited by 1,838
Animal Mitochondrial DNA: Structure and Evolution
Wolstenholme, D. R. (1992) · International review of cytology · doi:10.1016/s0074-7696(08)62066-5 · Cited by 1,714
THE MITOCHONDRIAL ELECTRON TRANSPORT AND OXIDATIVE PHOSPHORYLATION SYSTEM
Hatefi, Y. (1985) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.54.070185.005055 · Cited by 1,650
Mitochondrial transcription factor A is necessary for mtDNA maintance and embryogenesis in mice
Larsson, N.-G., Wang, J., Wilhelmsson, H., Oldfors, A., Rustin, P., Lewandoski, M., Barsh, G. S., & Clayton, D. A. (1998) · Nature Genetics · doi:10.1038/ng0398-231 · Cited by 1,594
Myoclonic epilepsy and ragged-red fiber disease (MERRF) is associated with a mitochondrial DNA tRNALys mutation
Shoffner, J. M., Lott, M. T., Lezza, A. M. S., Seibel, P., Ballinger, S. W., & Wallace, D. C. (1990) · Cell · doi:10.1016/0092-8674(90)90059-n · Cited by 1,476
Maternal inheritance of human mitochondrial DNA.
Giles, R. E., Blanc, H., Cann, H. M., & Wallace, D. C. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.11.6715 · Cited by 1,365
Replication of animal mitochondrial DNA
Clayton, D. A. (1982) · Cell · doi:10.1016/0092-8674(82)90049-6 · Cited by 1,243
Mutation in mitochondrial tRNALeu(UUR) gene in a large pedigree with maternally transmitted type II diabetes mellitus and deafness
van den Ouweland, J. M. W., Lemkes, H. H. P. J., Ruitenbeek, W., Sandkuijl, L. A., de Vijlder, M. F., Struyvenberg, P. A. A., van de Kamp, J. J. P., & Maassen, J. A. (1992) · Nature Genetics · doi:10.1038/ng0892-368 · Cited by 1,135
MITOCHONDRIAL DNA MAINTENANCE IN VERTEBRATES
Shadel, G. S., & Clayton, D. A. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.409 · Cited by 1,059
TRANSLATIONAL CONTROL IN MAMMALIAN CELLS
Hershey, J. W. B. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.003441 · Cited by 1,029
HMG domain proteins: architectural elements in the assembly of nucleoprotein structures
Grosschedl, R., Giese, K., & Pagel, J. M. (1994) · Trends in Genetics · doi:10.1016/0168-9525(94)90232-1 · Cited by 814
Mitochondrial DNA molecules and virtual number of mitochondria per cell in mammalian cells
Robin, E. D., & Wong, R. J. (1988) · Journal of Cellular Physiology · doi:10.1002/jcp.1041360316 · Cited by 660
Replication And Transcription Of Vertebrate Mitochondrial Dna
Clayton, D. A. (1991) · Annual Review of Cell Biology · doi:10.1146/annurev.cb.07.110191.002321 · Cited by 652
The Endosymbiont Hypothesis Revisited
Gray, M. W. (1992) · International Review of Cytology · doi:10.1016/s0074-7696(08)62068-9 · Cited by 586
mtDNA depletion with variable tissue expression: a novel genetic abnormality in mitochondrial diseases.
Moraes, C. T., Shanske, S., Tritschler, H., Aprille, J. R., Andreetta, F., Bonilla, E., Schon, E. A., & DiMauro, S. (1991) · PubMed · Cited by 586
Similarity of Human Mitochondrial Transcription Factor 1 to High Mobility Group Proteins
Parisi, M. A., & Clayton, D. A. (1991) · Science · doi:10.1126/science.2035027 · Cited by 548
Six unidentified reading frames of human mitochondrial DNA encode components of the respiratory-chain NADH dehydrogenase
Chomyn, A., Mariottini, P., Cleeter, M. W. J., RAGAN, C. I., Matsuno‐Yagi, A., Hatefi, Y., Doolittle, R. F., & Attardi, G. M. (1985) · Nature · doi:10.1038/314592a0 · Cited by 528
Maternal inheritance of mammalian mitochondrial DNA
Hutchison, C. A., Newbold, J. E., Potter, S. S., et al. (1974) · Nature · doi:10.1038/251536a0 · Cited by 517
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.
Chomyn, A., Martinuzzi, A., Yoneda, M., Daga, A., Hurko, O., Johns, D. R., Lai, S. T., Nonaka, I., Angelini, C. I., & Attardi, G. M. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.10.4221 · Cited by 491
EUKARYOTIC DNA POLYMERASES
Wang, T. S. ‐. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.002501 · Cited by 483
Elimination of paternal mitochondrial DNA in intraspecific crosses during early mouse embryogenesis.
Kaneda, H., Hayashi, J., Takahama, S., Taya, C., Lindahl, K. F., & Yonekawa, H. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.10.4542 · Cited by 462
Defects in mitochondrial protein synthesis and respiratory chain activity segregate with the tRNA(Leu(UUR)) mutation associated with mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes
King, M. P., Koga, Y., Davidson, M., & Schon, E. A. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.2.480 · Cited by 458
Sequence and properties of the human KB cell and mouse L cell D-loop regions of mitochondrial DNA
Walberg, M. W., & Clayton, D. A. (1981) · Nucleic Acids Research · doi:10.1093/nar/9.20.5411 · Cited by 362
Distinctive features of the 5′-terminal sequences of the human mitochondrial mRNAs
Montoya, J., Ojala, D., & Attardi, G. M. (1981) · Nature · doi:10.1038/290465a0 · Cited by 360
Recent evidence for evolution of the genetic code
Osawa, S., Jukes, T. H., Watanabe, K., & Muto, A. (1992) · Microbiological Reviews · doi:10.1128/mr.56.1.229-264.1992 · Cited by 357
DNA HELICASES
Matson, S. W., & Kaiser‐Rogers, K. A. (1990) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.59.070190.001445 · Cited by 355
Priming of human mitochondrial DNA replication occurs at the light-strand promoter.
Chang, D. D., & Clayton, D. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.2.351 · Cited by 349
URF6, Last Unidentified Reading Frame of Human mtDNA, Codes for an NADH Dehydrogenase Subunit
Chomyn, A., Cleeter, M. W. J., Ragan, C., Riley, M., Doolittle, R. F., & Attardi, G. M. (1986) · Science · doi:10.1126/science.3764430 · Cited by 348
Purification and characterization of human mitochondrial transcription factor 1.
Fisher, R. P., & Clayton, D. A. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.8.3496 · Cited by 347
Distribution and threshold expression of the tRNA(Lys) mutation in skeletal muscle of patients with myoclonic epilepsy and ragged-red fibers (MERRF).
Boulet, L., Karpati, G., & Shoubridge, E. A. (1992) · Europe PMC (PubMed Central) · Cited by 331
A close relative of the nuclear, chromosomal high-mobility group protein HMG1 in yeast mitochondria.
Diffley, J. F. X., & Stillman, B. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.17.7864 · Cited by 329
A mammalian Mitochondrial RNA Processing Activity Contains Nucleus-Encoded RNA
Chang, D. D., & Clayton, D. A. (1987) · Science · doi:10.1126/science.2434997 · Cited by 322
Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae
Schmitt, M., & Clayton, D. A. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7935-7941.1993 · Cited by 314
DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein.
Fisher, R. P., Lisowsky, T., Parisi, M. A., & Clayton, D. A. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50739-6 · Cited by 312
Elongation of displacement-loop strands in human and mouse mitochondrial DNA is arrested near specific template sequences.
Doda, J. N., Wright, C. T., & Clayton, D. A. (1981) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.78.10.6116 · Cited by 312
The pattern of transcription of the human mitochondrial rRNA genes reveals two overlapping transcription units
Montoya, J., Gaines, G. L., & Attardi, G. M. (1983) · Cell · doi:10.1016/0092-8674(83)90145-9 · Cited by 309
Identification of initiation sites for heavy-strand and light-strand transcription in human mitochondrial DNA.
Montoya, J., Christianson, T., Levens, D., Rabinowitz, M., & Attardi, G. M. (1982) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.79.23.7195 · Cited by 307
In Vitro Genetic Transfer of Protein Synthesis and Respiration Defects to Mitochondrial DNA-Less Cells with Myopathy-Patient Mitochondria
Chomyn, A., Meola, G., Bresolin, N., Lai, S. T., Scarlato, G., & Attardi, G. M. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.4.2236 · Cited by 301
Termination of transcription in human mitochondria: Identification and purification of a DNA binding protein factor that promotes termination
Kruse, B., MURDTER, N. N., & Attardi, G. M. (1989) · Cell · doi:10.1016/0092-8674(89)90853-2 · Cited by 300
Misconceptions about mitochondria and mammalian fertilization: Implications for theories on human evolution
Ankel‐Simons, F., & Cummins, J. M. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.24.13859 · Cited by 294
Accurate Processing of a Eukaryotic Precursor Ribosomal RNA by Ribonuclease MRP in Vitro
Lygerou, Z., Allmang, C., Tollervey, D., & Séraphin, B. (1996) · Science · doi:10.1126/science.272.5259.268 · Cited by 291
Codon recognition rules in yeast mitochondria.
Bonitz, S. G., Berlani, R. E., Coruzzi, G. M., Li, M., Macino, G., Nóbrega, F. G., Nóbrega, M. P., Thalenfeld, B. E., & Tzagoloff, A. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3167 · Cited by 288
MtDNA mutation in MERRF syndrome causes defective aminoacylation of tRNALys and premature translation termination
Enriquez, J. A., Chomyn, A., & Attardi, G. (1995) · Nature Genetics · doi:10.1038/ng0595-47 · Cited by 285
Cloning and Characterization of the Human Mitochondrial DNA Polymerase, DNA Polymerase γ
Ropp, P. A., & Copeland, W. C. (1996) · Genomics · doi:10.1006/geno.1996.0490 · Cited by 284
Different pattern of codon recognition by mammalian mitochondrial tRNAs.
Barrell, B. G., Anderson, S. K., Bankier, A. T., de Bruijn, M. H. L., Chen, E., Coulson, A. R., Drouin, J., Eperon, I. C., Nierlich, D. P., Roe, B. A., et al. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3164 · Cited by 270
Promoter selection in human mitochondria involves binding of a transcription factor to orientation-independent upstream regulatory elements
Fisher, R. P., Topper, J. N., & Clayton, D. A. (1987) · Cell · doi:10.1016/0092-8674(87)90220-0 · Cited by 256
Precise identification of individual promoters for transcription of each strand of human mitochondrial DNA.
Chang, D., & Clayton, D. A. (1984) · Cell · doi:10.1016/0092-8674(84)90343-x · Cited by 250
Novel features in the genetic code and codon reading patterns in Neurospora crassa mitochondria based on sequences of six mitochondrial tRNAs
Heckman, J. E., Sarnoff, J., Alzner-Deweerd, B., Yin, S., & RajBhandary, U. L. (1980) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.77.6.3159 · Cited by 246
The mitochondrial tRNA(Leu(UUR)) mutation in mitochondrial encephalomyopathy, lactic acidosis, and strokelike episodes (MELAS): genetic, biochemical, and morphological correlations in skeletal muscle.
Moraes, C. T., Ricci, E., Bonilla, E., DiMauro, S., & Schon, E. A. (1992) · PubMed · Cited by 244
Number of mitochondria and some properties of mitochondrial DNA in the mouse egg
Pikó, L., & Matsumoto, L. H. (1976) · Developmental Biology · doi:10.1016/0012-1606(76)90253-0 · Cited by 243
Primers for Mitochondrial DNA Replication Generated by Endonuclease G
Côté, J., & Ruiz-Carrillo, A. (1993) · Science · doi:10.1126/science.7688144 · Cited by 240
DNA polymerase of mitochondria is a gamma-polymerase.
Bolden, A. H., Noy, G. P., & Weissbach, A. (1977) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)40396-6 · Cited by 237
Impairment of mitochondrial transcription termination by a point mutation associated with the MELAS subgroup of mitochondrial encephalomyopathies
Hess, J. F., Parisi, M. A., Bennett, J. L., & Clayton, D. A. (1991) · Nature · doi:10.1038/351236a0 · Cited by 234
A novel endoribonuclease cleaves at a priming site of mouse mitochondrial DNA replication.
Chang, D., & Clayton, D. A. (1987) · EMBO Journal · doi:10.1002/j.1460-2075.1987.tb04770.x · Cited by 231
Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database.
Tiranti, V., Savoia, A., Forti, F., d'Apolito, M., Centra, M., Rocchi, M., & Zeviani, M. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.4.615 · Cited by 230
Both the conserved stem-loop and divergent 5'-flanking sequences are required for initiation at the human mitochondrial origin of light-strand DNA replication.
Hixson, J. E., Wong, T. W., & Clayton, D. A. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)35948-3 · Cited by 224
The RNA of RNase MRP is required for normal processing of ribosomal RNA.
Chu, S., Archer, R., Zengel, J., & Lindahl, L. (1994) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.91.2.659 · Cited by 222
A transcription factor required for promoter recognition by human mitochondrial RNA polymerase. Accurate initiation at the heavy- and light-strand promoters dissected and reconstituted in vitro.
Fisher, R. P., & Clayton, D. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39184-6 · Cited by 217
Low Levels of Mitochondrial Transcription Factor A in Mitochondrial DNA Depletion
Larsson, N., Oldfors, A., Holme, E., & Clayton, D. A. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1603 · Cited by 216
Synthesis and Turnover of Mitochondrial Ribonucleic Acid in HeLa Cells: the Mature Ribosomal and Messenger Ribonucleic Acid Species Are Metabolically Unstable
Gelfand, R., & Attardi, G. M. (1981) · Molecular and Cellular Biology · doi:10.1128/mcb.1.6.497 · Cited by 211
Replication priming and transcription initiate from precisely the same site in mouse mitochondrial DNA.
Chang, D. D., Hauswirth, W. W., & Clayton, D. A. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03817.x · Cited by 209
Cloning and Sequencing of the Nuclear Gene MIP1 Encoding the Catalytic Subunit of the Yeast Mitochondrial DNA Polymerase
Foury, F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)47098-1 · Cited by 208
Mitochondrial DNA copy number in bovine oocytes and somatic cells
Michaels, G. S., Hauswirth, W. W., & Laipis, P. J. (1982) · Developmental Biology · doi:10.1016/0012-1606(82)90088-4 · Cited by 207
Fate of the Sperm Mitochondria, and the Incorporation, Conversion, and Disassembly of the Sperm Tail Structures during Bovine Fertilization1
Šutovský, P., Navara, C. S., & Schatten, G. P. (1996) · Biology of Reproduction · doi:10.1095/biolreprod55.6.1195 · Cited by 206
Nuclear RNase MRP is required for correct processing of pre-5.8S rRNA in Saccharomyces cerevisiae.
Schmitt, M. E., & Clayton, D. A. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.12.7935 · Cited by 200
Counting target molecules by exponential polymerase chain reaction: Copy number of mitochondrial DNA in rat tissues
Wiesner, R. J., Rüegg, J. C., & Morano, I. (1992) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(92)90517-o · Cited by 197
Addition of a 29 Residue Carboxyl-terminal Tail Converts a Simple HMG Box-containing Protein into a Transcriptional Activator
Dairaghi, D. J., Shadel, G. S., & Clayton, D. A. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.9889 · Cited by 197
RNA‐DNA hybrid formation at the human mitochondrial heavy‐strand origin ceases at replication start sites: an implication for RNA‐DNA hybrids serving as primers.
Xu, B., & Clayton, D. A. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00676.x · Cited by 190
The human mitochondrial transcription termination factor (mTERF) is a multizipper protein but binds to DNA as a monomer, with evidence pointing to intramolecular leucine zipper interactions
Fernández‐Silva, P., Martínez‐Azorín, F., Micol, V., & Attardi, G. M. (1997) · The EMBO Journal · doi:10.1093/emboj/16.5.1066 · Cited by 190
In vitro replication of human mitochondrial DNA: Accurate initiation at the origin of light-strand synthesis
Wong, T. W., & Clayton, D. A. (1985) · Cell · doi:10.1016/0092-8674(85)90291-0 · Cited by 188
Mitochondrial transcription initiation. Variation and conservation
Shadel, G. S., & Clayton, D. A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)85387-5 · Cited by 185
A single‐stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB.
Dyck, E. V., Foury, F., Stillman, B., & Brill, S. J. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05421.x · Cited by 182
Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 Å resolution
Yang, C. L., Curth, U., Urbanke, C., & Kang, C. (1997) · Nature Structural Biology · doi:10.1038/nsb0297-153 · Cited by 179
DNA binding properties of an HMG1-related protein from yeast mitochondria.
Diffley, J. F. X., & Stillman, B. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)50740-2 · Cited by 175
Characterization of a histone-like protein extracted from yeast mitochondria.
Caron, F., Jacq, C., & Rouvière‐Yaniv, J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.9.4265 · Cited by 175
Deficiency of the human mitochondrial transcription factor h-mtTFA in infantile mitochondrial myopathy is associated with mtDNA depletion
Poulton, J., Morten, K., Emmerson, C. F., Potter, C., Sewry, C. A., Dubowitz, V., Kidd, H., Stephenson, J. R., Whitehouse, W. P., Hansen, F. J., et al. (1994) · Human Molecular Genetics · doi:10.1093/hmg/3.10.1763 · Cited by 169
Mitochondrial ribosomes
Borst, P., & Grivell, L. A. (1971) · FEBS Letters · doi:10.1016/0014-5793(71)80204-1 · Cited by 166
Maternal inheritance of the mouse mitochondrial genome is not mediated by a loss or gross alteration of the paternal mitochondrial DNA or by methylation of the oocyte mitochondrial DNA
Hecht, N. B., Liem, H., Kleene, K. C., et al. (1984) · Developmental Biology · doi:10.1016/0012-1606(84)90210-0 · Cited by 162
Biogenesis of mitochondria: the mitochondrial gene (aap1) coding for mitochondrial ATPase subunit 8 inSaccharomyces cerevisiae
Macreadie, I. G., Novitski, C. E., Maxwell, R. J., et al. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.13.4435 · Cited by 160
Characterization of an RNase P activity from HeLa cell mitochondria. Comparison with the cytosol RNase P activity.
Doersen, C., Guerrier-Takada, C., Altman, S., & Attardi, G. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88920-7 · Cited by 157
Symmetrical in vivo transcription of mitochondrial DNA in HeLa cells.
Aloni, Y., & Attardi, G. (1971) · Proceedings of the National Academy of Sciences of the United States of America · doi:10.1073/pnas.68.8.1757 · Cited by 152
Human Mitochondrial tRNA Processing
Rossmanith, W., Tullo, A., Potuschak, T., Karwan, R. M., & Sbis, E. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.21.12885 · Cited by 151
A single mouse gene encodes the mitochondrial transcription factor A and a testis–specific nuclear HMG-box protein
Larsson, N., Garman, J. D., Oldfors, A., Barsh, G. S., & Clayton, D. A. (1996) · Nature Genetics · doi:10.1038/ng0796-296 · Cited by 147
The yeast mitochondrial RNA polymerase specificity factor, MTF1, is similar to bacterial sigma factors.
Jang, S., & Jaehning, J. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54622-6 · Cited by 144
Purification and identification of subunit structure of the human mitochondrial DNA polymerase.
Gray, H. B., & Wong, T. W. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42629-4 · Cited by 140
Mitochondrial transcription initiation: promoter structures and RNA polymerases
Tracy, R. L., & Stern, D. B. (1995) · Current Genetics · doi:10.1007/bf00309779 · Cited by 140
Mitochondria
Galper, J., & Darnell, J. E., Jr. (1969) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(69)90633-0 · Cited by 133
Subcellular partitioning of MRP RNA assessed by ultrastructural and biochemical analysis
Li, K., Smagula, C., Parsons, W. J., Richardson, J. A., Gonzalez, M. A., Hagler, H. K., & Williams, R. S. (1994) · The Journal of Cell Biology · doi:10.1083/jcb.124.6.871 · Cited by 130
Protein composition of the bovine mitochondrial ribosome.
Matthews, D. E., Hessler, R. A., Denslow, N. D., Edwards, J. S., & O’Brien, T. W. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34199-1 · Cited by 128
Mechanism of replication of human mitochondrial DNA. Localization of the 5' ends of nascent daughter strands.
Tapper, D. P., & Clayton, D. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)69373-7 · Cited by 128
Evidence against a mitochondrial location of the 7-2/MRP RNA in mammalian cells
Kiss, T., & Filipowicz, W. (1992) · Cell · doi:10.1016/0092-8674(92)90528-k · Cited by 127
Protein translocation across mitochondrial membranes: What a long, strange trip it is
Ryan, K. R., & Jensen, R. E. (1995) · Cell · doi:10.1016/0092-8674(95)90089-6 · Cited by 126
Replication of Circular DNA in Eukaryotic Cells
Kasamatsu, H., & Vinograd, J. R. (1974) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.43.070174.003403 · Cited by 121
Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB)
Tiranti, V., Rocchi, M., DiDonato, S., & Zeviani, M. (1993) · Gene · doi:10.1016/0378-1119(93)90370-i · Cited by 120
Characterization of the yeast mitochondrial locus necessary for tRNA biosynthesis: DNA sequence analysis and identification of a new transcript
Miller, D. L., & Martín, N. C. R. (1983) · Cell · doi:10.1016/0092-8674(83)90548-2 · Cited by 119
Nuclear complementation restores mtDNA levels in cultured cells from a patient with mtDNA depletion.
Bodnar, A. G., Cooper, J. M., Holt, I. J., et al. (1993) · PubMed · Cited by 118
Molecular Mechanisms in Mitochondrial DNA Depletion Syndrome
Taanman, J., Bodnar, A. G., Cooper, J. M., et al. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.6.935 · Cited by 118
Self-citation
Mechanism of mitochondrial DNA replication in mouse L-cells: Localization and sequence of the light-strand origin of replication
Martens, P. A., & Clayton, D. A. (1979) · Journal of Molecular Biology · doi:10.1016/0022-2836(79)90440-6 · Cited by 118
Mitochondrial ribosomal proteins (MRPs) of yeast
Graack, H., & Wittmann‐Liebold, B. (1998) · Biochemical Journal · doi:10.1042/bj3290433 · Cited by 117
A Novel Modified Nucleoside Found at the First Position of the Anticodon of Methionine tRNA from Bovine Liver Mitochondria
Moriya, J., Yokogawa, T., Wakita, K., et al. (1994) · Biochemistry · doi:10.1021/bi00174a033 · Cited by 113
Fractionation of mitochondrial RNA from HeLa cells by high-resolution electrophoresis under strongly denaturing conditions
Amalric, F., Merkel, C., Gelfand, R., & Attardi, G. M. (1978) · Journal of Molecular Biology · doi:10.1016/0022-2836(78)90241-3 · Cited by 112
In Vitro Analysis of Mutations Causing Myoclonus Epilepsy with Ragged-Red Fibers in the Mitochondrial tRNALys Gene: Two Genotypes Produce Similar Phenotypes
Masucci, J. P., Davidson, M. M., Koga, Y., Schon, E. A., & King, M. P. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.5.2872 · Cited by 111
Yeast site-specific ribonucleoprotein endoribonuclease MRP contains an RNA component homologous to mammalian RNase MRP RNA and essential for cell viability.Preprint
Schmitt, M. E., & Clayton, D. A. (1992) · Genes & Development · doi:10.1101/gad.6.10.1975 · Cited by 109
Characterization of human MRP/Th RNA and its nuclear gene: full length MRP/Th RNA is an active endoribonuclease when assembled as an RNP
Topper, J. N., & Clayton, D. A. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.4.793 · Cited by 109
In Organello Footprint Analysis of Human Mitochondrial DNA: Human Mitochondrial Transcription Factor A Interactions at the Origin of Replication
Ghivizzani, S. C., Madsen, C. S., Nelen, M. R., Ammini, C. V., & Hauswirth, W. W. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.12.7717 · Cited by 107
Protein Binding to a Single Termination-Associated Sequence in the Mitochondrial DNA D-Loop Region
Madsen, C. S., Ghivizzani, S. C., & Hauswirth, W. W. (1993) · Molecular and Cellular Biology · doi:10.1128/mcb.13.4.2162-2171.1993 · Cited by 105
Delayed cytotoxicity and cleavage of mitochondrial DNA in ciprofloxacin-treated mammalian cells.
Lawrence, J. W., Claire, D., Weissig, V., & Rowe, T. C. (1996) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)09546-x · Cited by 104
In vitro transcription of human mitochondrial DNA. Identification of specific light strand transcripts from the displacement loop region.
Walberg, M. W., & Clayton, D. A. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)33188-0 · Cited by 103
A Tridecamer DNA Sequence Supports Human Mitochondrial RNA 3′-End Formation In Vitro
Christianson, T. W., & Clayton, D. A. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.10.4502-4509.1988 · Cited by 102
Chromosomal localization of mitochondrial transcription factor A (TCF6), single-stranded DNA-binding protein (SSBP), and Endonuclease G (ENDOG), three human housekeeping genes involved in mitochondrial biogenesis
Tiranti, V., Rossi, E. G., Ruiz-Carrillo, A., Rossi, G., Rocchi, M., DiDonato, S., Zuffardi, O., & Zeviani, M. (1995) · Genomics · doi:10.1016/0888-7543(95)80058-t · Cited by 101
Mitochondrial DNA polymerases from yeast to man: a new family of polymerases.
Lecrenier, N., van der Bruggen, P., & Foury, F. (1997) · Gene · doi:10.1016/s0378-1119(96)00663-4 · Cited by 100
Mitochondrial DNA Polymerase is Expressed and Translated in the Absence of Mitochondrial DNA Maintenance and Replication
Davis, A. F., Ropp, P. A., Clayton, D. A., & Copeland, W. C. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.14.2753 · Cited by 100
Single‐stranded‐DNA‐binding proteins from human mitochondria and Escherichia coli have analogous physicochemical properties
Curth, U., Urbanke, C., Greipel, J., Gerberding, H., Tiranti, V., & Zeviani, M. (1994) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1994.tb18756.x · Cited by 99
DNA primase of human mitochondria is associated with structural RNA that is essential for enzymatic activity
Wong, T. W., & Clayton, D. A. (1986) · Cell · doi:10.1016/0092-8674(86)90556-8 · Cited by 99
Molecular characterization of the transcription termination factor from human mitochondria.
Daga, A., Micol, V., Hess, D., Aebersold, R. H., & Attardi, G. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53070-2 · Cited by 98
Mitochondrial DNA in anucleate human blood cells
Shuster, R. C., Rubenstein, A. J., & Wallace, D. C. (1988) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(88)81291-9 · Cited by 97
Liver failure associated with mitochondrial DNA depletion
Morris, A. A. M., Taanman, J., Blake, J. C., Cooper, J. A. D., Lake, B. D., Malone, M., Love, S., Clayton, P. T., Leonard, J. V., & Schapira, A. H. V. (1998) · Journal of Hepatology · doi:10.1016/s0168-8278(98)80278-x · Cited by 97
Self-citation
Differential Expression of Mitochondrial DNA Replication Factors in Mammalian Tissues
Schultz, R. A., Swoap, S. J., McDaniel, L. D., et al. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3447 · Cited by 94
Strictly maternal inheritance of rat mitochondrial DNA
Hayashi, J., Yonekawa, H., Gotoh, O., Watanabe, J. A., & Tagashira, Y. (1978) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(78)91499-7 · Cited by 93
RNase mitochondrial RNA processing correctly cleaves a novel R loop at the mitochondrial DNA leading-strand origin of replication.Preprint
Lee, D. Y., & Clayton, D. A. (1997) · Genes & Development · doi:10.1101/gad.11.5.582 · Cited by 91
A nuclear gene essential for mitochondrial replication suppresses a defect of mitochondrial transcription in Saccharomyces cerevisiae
Lisowsky, T., & Michaelis, G. (1988) · Molecular and General Genetics MGG · doi:10.1007/bf00337714 · Cited by 90
Identification of a promoter for transcription of the heavy strand of human mtDNA: In vitro transcription and deletion mutagenesis
Bogenhagen, D. F., Applegate, E. F., & Yoza, B. K. (1984) · Cell · doi:10.1016/0092-8674(84)90061-8 · Cited by 89
Down-Regulation of Mitochondrial Transcription Factor a During Spermatogenesis in Humans
Larsson, N., Oldfors, A., Garman, J. D., Barsh, G. S., & Clayton, D. A. (1997) · Human Molecular Genetics · doi:10.1093/hmg/6.2.185 · Cited by 89
Bovine mitochondrial protein synthesis elongation factors. Identification and initial characterization of an elongation factor Tu-elongation factor TS complex
Spremulli, L. L., & Schwartzbach, C. J. (2021) · PubMed · doi:10.17615/7m2f-aj33 · Cited by 89
A role for RNAse MRP in mitochondrial RNA processing
Topper, J. N., Bennett, J. L., & Clayton, D. A. (1992) · Cell · doi:10.1016/0092-8674(92)90529-l · Cited by 88
Human mitochondrial transcription factor A and promoter spacing integrity are required for transcription initiation
Dairaghi, D. J., Shadel, G. S., & Clayton, D. A. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00019-z · Cited by 87
Expression, Purification, and Initial Kinetic Characterization of the Large Subunit of the Human Mitochondrial DNA Polymerase
Graves, S. W., Johnson, A. A., & Johnson, K. A. (1998) · Biochemistry · doi:10.1021/bi972685u · Cited by 87
Stoichiometry of Mitochondrial Transcripts and Regulation of Gene Expression by Mitochondrial Transcription Factor A
Garstka, H. L., Fäcke, M., Escribano, J., et al. (1994) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1994.1493 · Cited by 86
Distinct Roles for Two Purified Factors in Transcription of Xenopus Mitochondrial DNA
Antoshechkin, I. A., & Bogenhagen, D. F. (1995) · Molecular and Cellular Biology · doi:10.1128/mcb.15.12.7032 · Cited by 82
Evidence for complete symmetrical transcription in vivo of mitochondrial DNA in HeLa cells
Murphy, W. I., Attardi, B., Tu, C., & Attardi, G. M. (1975) · Journal of Molecular Biology · doi:10.1016/s0022-2836(75)80187-2 · Cited by 81
Cloning, sequence analysis and expression of mammalian mitochondrial protein synthesis elongation factor Tu
Woriax, V. L., Burkhart, W., & Spremulli, L. L. (1995) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(95)00176-x · Cited by 80
Initiation of transcription from each of the two human mitochondrial promoters requires unique nucleotides at the transcriptional start sites.
Hixson, J. E., & Clayton, D. A. (1985) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.82.9.2660 · Cited by 79
Assignment of a yeast protein necessary for mitochondrial transcription initiation
Xu, B., & Clayton, D. A. (1992) · Nucleic Acids Research · doi:10.1093/nar/20.5.1053 · Cited by 78
In vitro transcription of human mitochondrial DNA: accurate termination requires a region of DNA sequence that can function bidirectionally.
Christianson, T. W., & Clayton, D. A. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.17.6277 · Cited by 77
Markedly different ATP requirements for rRNA synthesis and mtDNA light strand transcription versus mRNA synthesis in isolated human mitochondria.
Gaines, G., Rossi, C., & Attardi, G. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)75725-1 · Cited by 76
Sequence analysis and precise mapping of the 3′ ends of HeLa cell mitochondrial ribosomal RNAs
Dubin, D. T., Montoya, J., Timko, K. D., et al. (1982) · Journal of Molecular Biology · doi:10.1016/0022-2836(82)90510-1 · Cited by 76
Mitochondrial DNA and RNA processing in MELAS
Kaufmann, P., Shanske, S., Hirano, M., DiMauro, S., King, M. P., Koga, Y., & Schon, E. A. (1996) · Annals of Neurology · doi:10.1002/ana.410400208 · Cited by 75
The mitochondrial tRNALeu(UUR) mutation in MELAS: a model for pathogenesis
Schon, E. A., Koga, Y., Davidson, M. M., Moraes, C. T., & King, M. P. (1992) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(92)90226-r · Cited by 74
The Fate of Human Sperm-Derived mtDNA in Somatic Cells
Manfredi, G., Thyagarajan, D. E., Papadopoulou, L. C., Pallotti, F., & Schon, E. A. (1997) · The American Journal of Human Genetics · doi:10.1086/514887 · Cited by 74
A common core for binding single‐stranded DNA: structural comparison of the single‐stranded DNA‐binding proteins (SSB) from E. coli and human mitochondria
Webster, G. D., Genschel, J., Curth, U., et al. (1997) · FEBS Letters · doi:10.1016/s0014-5793(97)00747-3 · Cited by 71
Construction of a yeast mutant lacking the mitochondrial nuclease
Zassenhaus, H. P., Hofmann, T. J., Uthayashanker, R. E., Vincent, R. D., & Zona, M. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.8.3283 · Cited by 71
Fate of sperm tail components after incorporation into the hamster egg
Hiraoka, J.-I., & Hirao, Y.-H. (1988) · Gamete Research · doi:10.1002/mrd.1120190408 · Cited by 69
Yeast mitochondrial RNase P. Sequence of the RPM2 gene and demonstration that its product is a protein subunit of the enzyme.
Dang, Y. L., & Martin, N. C. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)36583-4 · Cited by 68
Purification and characterization of the potent endonuclease in extracts of bovine heart mitochondria.
Cummings, O. W., King, T. C., Holden, J. A., et al. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61611-4 · Cited by 65
N-formylmethionyl transfer ribonucleic acid in mitochondria from Neurospora
Epler, J. L., Shugart, L. R., & Barnett, W. E. (1970) · Biochemistry · doi:10.1021/bi00820a011 · Cited by 63
Mitochondrial Ribosomes in HeLa Cells
Attardi, G. M., & Ojala, D. (1971) · Nature New Biology · doi:10.1038/newbio229133a0 · Cited by 62
A Disease-Associated G5703A Mutation in Human Mitochondrial DNA Causes a Conformational Change and a Marked Decrease in Steady-State Levels of Mitochondrial tRNA Asn
Hao, H., & Moraes, C. T. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.12.6831 · Cited by 61
Initiation of protein synthesis in animal mitochondria. Purification and characterization of translational initiation factor 2.
Liao, H. X., & Spremulli, L. L. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54767-0 · Cited by 60
A rapid, efficient method for purifying DNA-binding proteins. Denaturation-renaturation chromatography of human and yeast mitochondrial extracts
Fisher, R. P., Lisowsky, T., Breen, G. A., & Clayton, D. A. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)31564-3 · Cited by 60
Intercalating drugs and low temperatures inhibit synthesis and processing of ribosomal RNA in isolated human mitochondria
Gaines, G., & Attardi, G. M. (1984) · Journal of Molecular Biology · doi:10.1016/s0022-2836(84)80017-0 · Cited by 60
Regulation of the expression of mitochondrial proteins: relationship between mtDNA copy number and cytochrome-c oxidase activity in human cells and tissues
den Bogert, C. V., Vries, H. D., Holtrop, M. E., Muus, P., Dekker, H. L., Galen, M. J. M. V., Bolhuis, P. A., & Taanman, J. (1993) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(93)90170-k · Cited by 60
Self-citation
Cloning and Expression of Mitochondrial Translational Elongation Factor Ts from Bovine and Human Liver
Xin, H., Woriax, V. L., Burkhart, W., et al. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.29.17243 · Cited by 60
Functional and Molecular Mitochondrial Abnormalities Associated with a C → T Transition at Position 3256 of the Human Mitochondrial Genome
Hao, H., & Moraes, C. T. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.4.2347 · Cited by 59
A tridecamer DNA sequence supports human mitochondrial RNA 3'-end formation in vitro.
Christianson, T. W., & Clayton, D. A. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.10.4502 · Cited by 58
A MOLECULAR GENETIC STUDY OF FOCAL HISTOCHEMICAL DEFECTS IN MITOCHONDRIAL ENCEPHALOMYOPATHIES
Hammans, S. R., Sweeney, M. G., Wicks, D., et al. (1992) · Brain · doi:10.1093/brain/115.2.343 · Cited by 57
The heterogeneity of rat-liver mitochondrial DNA
Kroon, A. M., de Vos, W. M., & Bakker, H. (1978) · Biochimica et Biophysica Acta (BBA) - Nucleic Acids and Protein Synthesis · doi:10.1016/0005-2787(78)90079-5 · Cited by 56
Dramatic size variation of yeast mitochondrial RNAs suggests that RNase P RNAs can be quite small.
Wise, C. A., & Martin, N. C. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54974-7 · Cited by 54
Identification and initial characterization of translational initiation factor 2 from bovine mitochondria.
Liao, H. X., & Spremulli, L. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77393-6 · Cited by 54
Ultracentrifugal characterization of the mitochondrial ribosome and subribosomal particles of bovine liver. Molecular size and composition
Hamilton, M. G., & O’Brien, T. W. (1974) · Biochemistry · doi:10.1021/bi00723a024 · Cited by 54
Analysis of cybrids harboring MELAS mutations in the mitochondrial tRNALeu(UUR) gene
Koga, Y., Davidson, M. M., Schon, E. A., & King, M. P. (1995) · Muscle & Nerve · doi:10.1002/mus.880181424 · Cited by 54
Structural and functional studies of the rat mitochondrial single strand DNA binding protein P16
Hoke, G. D., Pavco, P. A., Ledwith, B. J., & Tuyle, G. C. V. (1990) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(90)90094-f · Cited by 53
Synthesis and turnover rates of four rat liver mitochondrial RNA species
Cantatore, P., Flagella, Z., Fracasso, F., et al. (1987) · FEBS Letters · doi:10.1016/0014-5793(87)81480-1 · Cited by 53
Human mitochondrial transcription termination exhibits RNA polymerase independence and biased bipolarity in vitro.
Shang, J., & Clayton, D. A. (1994) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)62019-3 · Cited by 52
Identification and in vitro capping of a primary transcript of human mitochondrial DNA.
Yoza, B. K., & Bogenhagen, D. F. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)43183-8 · Cited by 52
Molecular recognition governing the initiation of translation in Escherichia coli. A review
Schmitt, E., Guillon, J. M., Meinnel, T., et al. (1996) · Biochimie · doi:10.1016/s0300-9084(96)80001-0 · Cited by 52
Endonuclease G from mammalian nuclei is identical to the major endonuclease of mitochondria
Gerschenson, M., Houmiel, K. L., & Low, R. L. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.1.88 · Cited by 51
Multiple Protein-Binding Sites in the TAS-Region of Human and Rat Mitochondrial DNA
Roberti, M., Musicco, C., Polosa, P. L., Milella, F., Gadaleta, M. N., & Cantatore, P. (1998) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.8052 · Cited by 51
Cloning and Sequence Analysis of the Human Mitochondrial Translational Initiation Factor 2 cDNA
Ma, L., & Spremulli, L. L. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1859 · Cited by 50
Failure to detect “cap” structures in mitochondrial DNA-coded poly(A)-containing RNA from HeLa cells
Grohmann, K., Amalric, F., Crews, S. T., & Attardi, G. M. (1978) · Nucleic Acids Research · doi:10.1093/nar/5.3.637 · Cited by 50
Mitochondrial poly(A) polymerase from a poorly differentiated hepatoma. Purification and characteristics
Rose, K. M., Morris, H. P., & Jacob, S. T. (1975) · Biochemistry · doi:10.1021/bi00676a022 · Cited by 50
The gamma subfamily of DNA polymerases: cloning of a developmentally regulated cDNA encoding Xenopus laevis mitochondrial DNA polymerase gamma
Ye, F. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.8.1481 · Cited by 50
Replication-Competent Human Mitochondrial DNA Lacking the Heavy-Strand Promoter Region
Moraes, C. T., Andreetta, F., Bonilla, E., Shanske, S., DiMauro, S., & Schon, E. A. (1991) · Molecular and Cellular Biology · doi:10.1128/mcb.11.3.1631 · Cited by 48
Purification and characterization of elongation factor G from bovine liver mitochondria.
Chung, H.-J., & Spremulli, L. L. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)45317-8 · Cited by 47
Interaction of bovine mitochondrial ribosomes with messenger RNA
Liao, H. X., & Spremulli, L. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83265-3 · Cited by 46
Interaction of mtTFB and mtRNA Polymerase at Core Promoters for Transcription of Xenopus laevis mtDNA
Bogenhagen, D. F. (1996) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)82655-2 · Cited by 45
Identification of transcriptional regulatory elements in human mitochondrial DNA by linker substitution analysis.
Topper, J. N., & Clayton, D. A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.3.1200 · Cited by 45
5-[[(Carboxymethyl)amino]methyl]uridine is found in the anticodon of yeast mitochondrial tRNAs recognizing two-codon families ending in a purine
Martin, R. P., Sibler, A. P., Gehrke, C. W., et al. (1990) · Biochemistry · doi:10.1021/bi00456a016 · Cited by 45
The presence of two mitochondrial DNA topoisomerases in human acute leukemia cells
Castora, F. J., Lazarus, G. M., & Kunes, D. (1985) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(85)90495-4 · Cited by 45
Fine mapping of mitochondrial RNAs derived from the mtDNA region containing a point mutation associated with MELAS
Koga, Y., Davidson, M. M., Schon, E. A., & King, M. P. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.3.657 · Cited by 44
Stimulation of Drosophila Mitochondrial DNA Polymerase by Single-stranded DNA-binding Protein
Williams, A. J., & Kaguni, L. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.2.860 · Cited by 43
Identification of the 3‘-ends of the two mouse mitochondrial ribosomal RNAs. The 3‘-end of 16 S ribosomal RNA contains nucleotides encoded by the gene for transfer RNALeuUUR.
Etten, R. A. V., Bird, J., & Clayton, D. A. (1983) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)44611-4 · Cited by 42
The human mitochondrial elongation factor tu (EF-Tu) gene: cDNA sequence, genomic localization, genomic structure, and identification of a pseudogene
Ling, M., Merante, F., Chen, H.-S., Duff, C. L., Duncan, A. M. V., & Robinson, B. H. (1997) · Gene · doi:10.1016/s0378-1119(97)00279-5 · Cited by 42
Expression, Purification, and Mechanistic Studies of Bovine Mitochondrial Translational Initiation Factor 2
Ma, J., & Spremulli, L. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.10.5805 · Cited by 42
Search for a DNA gyrase in mammalian mitochondria.
Castora, F. J., & Simpson, M. V. (1979) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)86467-0 · Cited by 41
Subunit Structure of Mitochondrial DNA Polymerase from Drosophila Embryos
Olson, M. W., Wang, Y., Elder, R. H., & Kaguni, L. S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.48.28932 · Cited by 40
Isolation and Characterization of Rat Liver Mitochondrial Ribosomes
Cahill, A., Baio, D. L., & CUNNINGHAM, C. C. (1995) · Analytical Biochemistry · doi:10.1006/abio.1995.9962 · Cited by 40
Mechanism of mRNA binding to bovine mitochondrial ribosomes
Denslow, N. D., Michaels, G. S., Montoya, J., et al. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83186-6 · Cited by 39
Mechanistic studies of the translational elongation cycle in mammalian mitochondria
Woriax, V. L., Bullard, J. M., Ma, L., et al. (1997) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(97)00002-x · Cited by 39
A mitochondrial elongation factor‐like protein is over‐expressed in tumours and differentially expressed in normal tissues
Wells, J. M., Henkler, F., Leversha, M. A., & Koshy, R. (1995) · FEBS Letters · doi:10.1016/0014-5793(94)01403-n · Cited by 38
The gene for the RNA component of the mitochondrial RNA-processing endoribonuclease is located on human chromosome 9p and on mouse chromosome 4
Hsieh, C., Donlon, T. A., Darras, B. T., et al. (1990) · Genomics · doi:10.1016/0888-7543(90)90483-b · Cited by 38
Functional Analysis of in Vivo and in Organello Footprinting of HeLa Cell Mitochondrial DNA in Relationship to ATP and Ethidium Bromide Effects on Transcription
Micol, V., Fernández‐Silva, P., & Attardi, G. M. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.30.18896 · Cited by 38
The HMG‐box mitochondrial transcription factor xl‐mtTFA binds DNA as a tetramer to activate bidirectional transcription
Antoshechkin, I. A., Bogenhagen, D. F., & Mastrangelo, I. A. (1997) · The EMBO Journal · doi:10.1093/emboj/16.11.3198 · Cited by 37
Minor Transcription Initiation Events Indicate that Both Human Mitochondrial Promoters Function Bidirectionally
Chang, D. D., Hixson, J. E., & Clayton, D. A. (1986) · Molecular and Cellular Biology · doi:10.1128/mcb.6.1.294-301.1986 · Cited by 37
Respiratory-deficient human fibroblasts exhibiting defective mitochondrial DNA replication
Bodnar, A. G., Cooper, J. A. D., Leonard, J. V., & Schapira, A. H. V. (1995) · Biochemical Journal · doi:10.1042/bj3050817 · Cited by 36
Ribonucleoprotein Particles involved in HeLa Mitochondrial Protein Synthesis
Brega, A., & Vesco, C. (1971) · Nature New Biology · doi:10.1038/newbio229136a0 · Cited by 36
DNA helicase from mammalian mitochondria.
Hehman, G. L., & Hauswirth, W. W. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8562 · Cited by 32
Upstream region of a genomic gene for human mitochondrial transcription factor 1
Tominaga, K., Akiyama, S., Kagawa, Y., et al. (1992) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/0167-4781(92)90082-b · Cited by 31

Research works printed but not linked: 9

Carrodeguas, 1996, Gene Express., 6, 219
Moraes, 1992, Am. J. Hum. Genet., 50, 934
Schwartzbach, 1989, J. Biol. Chem., 264, 19125, 10.1016/S0021-9258(19)47276-1 · DOI
Boulet, 1992, Am. J. Hum. Genet., 51, 1187
Schon, 1992, Biochim. Biophys. Acta, 1101, 206
Madsen, 1993, Mol. Cell. Biol., 13, 2162, 10.1128/MCB.13.4.2162 · DOI
Lawrence, 1996, Mol. Pharmacol., 50, 1178
Moraes, 1991, Am. J. Hum. Genet., 48, 492
Bodnar, 1993, Am. J. Hum. Genet., 53, 663

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Zhang, Q., Raoof, M., Chen, Y., Sumi, Y., Sursal, T., Junger, W., Brohi, K., Itagaki, K., & Hauser, C. J. (2010) · Nature · doi:10.1038/nature08780 · Cited by 3,812
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Mitochondrial DNA that escapes from autophagy causes inflammation and heart failure
Oka, T., Hikoso, S., Yamaguchi, O., Taneike, M., Takeda, T., Tamai, T., Oyabu, J., Murakawa, T., Nakayama, H., Nishida, K., et al. (2012) · Nature · doi:10.1038/nature10992 · Cited by 1,201
Transcriptional integration of mitochondrial biogenesis
Scarpulla, R. C., Vega, R. B., & Kelly, D. P. (2012) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2012.06.006 · Cited by 798
Proteomic Mapping of the Human Mitochondrial Intermembrane Space in Live Cells via Ratiometric APEX Tagging
Hung, V., Zou, P., Rhee, H.-W., Udeshi, N. D., Cracan, V., Svinkina, T., Carr, S. A., Mootha, V. K., & Ting, A. Y. (2014) · Molecular Cell · doi:10.1016/j.molcel.2014.06.003 · Cited by 517

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Authors: Taanman, J.-W.
Affiliations: University of London (GB)
Corresponding author: Taanman, Jan-Willem
ORCID: Taanman, Jan-Willem
Venue: Biochimica et Biophysica Acta (BBA) - Bioenergetics
Publisher: Elsevier BV
Published: 1999-02
Volume: 1410
Issue: 2
Pages: 103-123
ISSN: 0005-2728 (ISSN-L)
DOI: 10.1016/s0005-2728(98)00161-3
OpenAlex: W2038481472
Cited by: 1,635
References: 220
Citations by year: 2026: 57 · 2025: 89 · 2024: 101 · 2023: 132 · 2022: 113 · 2021: 126 · 2020: 89 · 2019: 122 · 2018: 105 · 2017: 92 · 2016: 69 · 2015: 52 · 2014: 57 · 2013: 47 · 2012: 37
FWCI: 1.56
Type: journal article
Language: en
Open access: bronze
doi.org
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 5281 d)
Locations: Biochimica et Biophysica Acta (BBA) - Bioenergetics (publishedVersion)
PubMed (publishedVersion)
UCL Discovery (University College London) (submittedVersion)
Funders: Wellcome Trust (048410)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › ATP Synthase and ATPases Research
Keywords: mitochondrial DNA, mitochondrial genome structure, mitochondrial transcription, mitochondrial translation, mitochondrial DNA replication, oxidative phosphorylation, mitochondrial gene expression, mitochondrial DNA mutations, cis-regulatory elements, trans-acting factors, mitochondrial disease, maternal inheritance, mitochondrial protein import
MeSH terms: Cells, Cultured, DNA Replication, DNA, Mitochondrial, Humans, Transcription, Genetic, Protein Biosynthesis, Molecular Structure

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The mitochondrial genome: structure, transcription, translation and replication

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