Cited by 415Mitochondrial Function and PathologyDNA Repair MechanismsDNA and Nucleic Acid Chemistry

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DNA Polymerase γ, The Mitochondrial Replicase

Kaguni, Laurie S.·2004·Annual Review of Biochemistry

DOI 10.1146/annurev.biochem.72.121801.161455

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Abstract

DNA polymerase (pol) gamma is the sole DNA polymerase in animal mitochondria. Biochemical and genetic evidence document a key role for pol gamma in mitochondrial DNA replication, and whereas DNA repair and recombination were thought to be limited or absent in animal mitochondria, both have been demonstrated in recent years. Thus, the mitochondrial replicase is also apparently responsible for the relevant DNA synthetic reactions in these processes. Pol gamma comprises a catalytic core in a heterodimeric complex with an accessory subunit. The two-subunit holoenzyme is an efficient and processive polymerase, which exhibits high fidelity in nucleotide selection and incorporation while proofreading errors with its intrinsic 3' 5' exonuclease. Incorporation of nucleotide analogs followed by proofreading failure leads to mitochondrial toxicity in antiviral therapy, and misincorporation during DNA replication leads to mitochondrial mutagenesis and dysfunction. This review describes our current understanding of pol gamma biochemistry and biology, and it introduces other key proteins that function at the mitochondrial DNA replication fork.

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures
Kraulis, P. J. (1991) · Journal of Applied Crystallography · doi:10.1107/s0021889891004399 · Cited by 14,011
[26] Raster3D: Photorealistic molecular graphics
Merritt, E. A., & Bacon, D. (1997) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/s0076-6879(97)77028-9 · Cited by 3,749
Rapid evolution of animal mitochondrial DNA
Brown, W. M., George, M., & Wilson, A. C. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.4.1967 · Cited by 3,439
Cellular roles of DNA topoisomerases: a molecular perspective
Wang, J. C. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm831 · Cited by 2,364
Diseases of the mitochondrial DNA
Wallace, D. C. (1992) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.61.070192.005523 · Cited by 1,319
Replication of animal mitochondrial DNA
Clayton, D. A. (1982) · Cell · doi:10.1016/0092-8674(82)90049-6 · Cited by 1,243
Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
Doublié, S., Tabor, S., Long, A. M., Richardson, C. C., & Ellenberger, T. (1998) · Nature · doi:10.1038/34593 · Cited by 1,184
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
Thymidine Phosphorylase Gene Mutations in MNGIE, a Human Mitochondrial Disorder
Nishino, I., Spinazzola, A., & Hirano, M. (1999) · Science · doi:10.1126/science.283.5402.689 · Cited by 899
Human mitochondrial DNA deletions associated with mutations in the gene encoding twinkle, a phage T7 gene 4-like protein localized in mitochondria
Spelbrink, J. N., Li, F.-Y., Tiranti, V., Nikali, K., Yuan, Q.-P., Tariq, M., Wanrooij, S., Garrido, N., Comi, G., Morandi, L., et al. (2001) · Nature Genetics · doi:10.1038/90058 · Cited by 882
Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
Ollis, D. L., Brick, P., Hamlin, R. C., Xuong, N., & Steitz, T. A. (1985) · Nature · doi:10.1038/313762a0 · Cited by 848
DNA Polymerases: Structural Diversity and Common Mechanisms
Steitz, T. A. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.25.17395 · Cited by 848
Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions
Van Goethem, G., Dermaut, B., Löfgren, A., Martin, J.-J., & Van Broeckhoven, C. (2001) · Nature Genetics · doi:10.1038/90034 · Cited by 841
Mitochondrial Myopathy Caused by Long-Term Zidovudine Therapy
Dalakas, M. C., Illa, I., Pezeshkpour, G. H., Laukaitis, J. P., Cohen, B. H., & Griffin, J. L. (1990) · New England Journal of Medicine · doi:10.1056/nejm199004193221602 · Cited by 837
Error-Prone Repair DNA Polymerases in Prokaryotes and Eukaryotes
Goodman, M. F. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.083101.124707 · Cited by 727
FIDELITY MECHANISMS IN DNA REPLICATION
Echols, H., & Goodman, M. F. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.002401 · Cited by 712
Eukaryotic DNA Polymerases
Hübscher, U., Maga, G., & Spadari, S. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.090501.150041 · Cited by 691
Role of Adenine Nucleotide Translocator 1 in mtDNA Maintenance
Kaukonen, J., Juselius, J. K., Tiranti, V., Kyttälä, A., Zeviani, M., Comi, G. P., Keränen, S., Peltonen, L., & Suomalainen, A. (2000) · Science · doi:10.1126/science.289.5480.782 · Cited by 641
An attempt to unify the structure of polymerases
Delarue, M. H., Poch, O., Tordo, N., Moras, D., & Argos, P. (1990) · Protein Engineering Design and Selection · doi:10.1093/protein/3.6.461 · Cited by 638
Pharmacology of nucleoside and nucleotide reverse transcriptase inhibitor-induced mitochondrial toxicity
Kakuda, T. N. (2000) · Clinical Therapeutics · doi:10.1016/s0149-2918(00)90004-3 · Cited by 617
Hepatic failure and lactic acidosis due to fialuridine (FIAU), an investigational nucleoside analogue for chronic hepatitis B
McKenzie, R., Fried, M. W., Sallie, R., Conjeevaram, H., Di Bisceglie, A. M., Park, Y., Savarese, B., Kleiner, D., Tsokos, M., Luciano, C., et al. (1995) · New England Journal of Medicine · doi:10.1056/nejm199510263331702 · Cited by 616
Visualizing DNA replication in a catalytically active Bacillus DNA polymerase crystal
Kiefer, J. R., Mao, C., Braman, J. C., & Beese, L. S. (1998) · Nature · doi:10.1038/34693 · Cited by 518
Mitochondrial toxicity of nrti antiviral drugs: an integrated cellular perspective
Lewis, W., Day, B. J., & Copeland, W. C. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd1201 · Cited by 496
EUKARYOTIC DNA POLYMERASES
Wang, T. S. ‐. (1991) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.60.070191.002501 · Cited by 483
Crystal Structure of a pol α Family Replication DNA Polymerase from Bacteriophage RB69
Wang, J., Sattar, A. K. M. A., Wang, C. C., Karam, J. D., Konigsberg, W. H., & Steitz, T. A. (1997) · Cell · doi:10.1016/s0092-8674(00)80296-2 · Cited by 430
Coupled Leading- and Lagging-Strand Synthesis of Mammalian Mitochondrial DNA
Holt, I. J., Lorimer, H. E., & Jacobs, H. T. (2000) · Cell · doi:10.1016/s0092-8674(00)80688-1 · Cited by 418
Toxicity of Antiviral Nucleoside Analogs and the Human Mitochondrial DNA Polymerase
Johnson, A. A., Ray, A. S., Hanes, J. W., Suo, Z., Colacino, J. M., Anderson, K. S., & Johnson, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106743200 · Cited by 399
Composition and dynamics of human mitochondrial nucleoids.
Garrido, N., Griparić, L., Jokitalo, E., Wartiovaara, J., van der Bliek, A. M., & Spelbrink, J. (2003) · Molecular Biology of the Cell · doi:10.1091/mbc.e02-07-0399 · Cited by 390
Crystal structure of Thermus aquaticus DNA polymerase
Kim, Y., Eom, S. H., Wang, J., Lee, D., Suh, S. W., & Steitz, T. A. (1995) · Nature · doi:10.1038/376612a0 · Cited by 360
Failure to produce mitochondrial DNA results in embryonic lethality in Rnaseh1 null mice
Cerritelli, S. M., Frolova, E. G., Feng, C., Grinberg, A., Love, P. E., & Crouch, R. J. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00088-1 · Cited by 358
Compilation and alignment of DNA polymerase sequences
Ito, J., & Braithwaite, D. K. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.15.4045 · Cited by 337
Chemical and physical fixation of isolated mitochondria in low-energy and high-energy states.
Hackenbrock, C. R. (1968) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.61.2.598 · Cited by 337
TWINKLE Has 5' −>3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein
Korhonen, J. A., Gaspari, M., & Falkenberg, M. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306981200 · Cited by 298
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
A Unified Polymerase Mechanism for Nonhomologous DNA and RNA Polymerases
Steitz, T. A., Smerdon, S. J., Jäger, J., & Joyce, C. M. (1994) · Science · doi:10.1126/science.7528445 · Cited by 280
The 3′‐5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction.
Derbyshire, V., Grindley, N. D. F., & Joyce, C. M. (1991) · The EMBO Journal · doi:10.1002/j.1460-2075.1991.tb07916.x · Cited by 278
Biased Incorporation of Ribonucleotides on the Mitochondrial L-Strand Accounts for Apparent Strand-Asymmetric DNA Replication
Yang, M., Bowmaker, M., Reyes, A., Vergani, L., Angeli, P., Gringeri, E., Jacobs, H. T., & Holt, I. J. (2002) · Cell · doi:10.1016/s0092-8674(02)01075-9 · Cited by 275
The Fidelity of Human DNA Polymerase γ with and without Exonucleolytic Proofreading and the p55 Accessory Subunit
Longley, M. J., Nguyen, D., Kunkel, T. A., & Copeland, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105230200 · Cited by 270
Mutations of mitochondrial DNA polymerase γA are a frequent cause of autosomal dominant or recessive progressive external ophthalmoplegia
Lamantea, E., Tiranti, V., Bordoni, A., Toscano, A., Bono, F., Servidei, S., Papadimitriou, A., Spelbrink, H., Silvestri, L., Casari, G., et al. (2002) · Annals of Neurology · doi:10.1002/ana.10278 · Cited by 270
Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli.
Polesky, A. H., Steitz, T. A., Grindley, N. D. F., & Joyce, C. M. (1990) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)77342-0 · Cited by 259
The Human DNA Ligase III Gene Encodes Nuclear and Mitochondrial Proteins
Lakshmipathy, U., & Campbell, C. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.5.3869 · Cited by 243
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
Identification of 5′-deoxyribose phosphate lyase activity in human DNA polymerase γ and its role in mitochondrial base excision repair in vitro
Longley, M. J., Prasad, R., Srivastava, D., Wilson, S. H., & Copeland, W. C. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.21.12244 · Cited by 228
Differential Incorporation and Removal of Antiviral Deoxynucleotides by Human DNA Polymerase γ
Lim, S. E., & Copeland, W. C. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101114200 · Cited by 227
The Mitochondrial p55 Accessory Subunit of Human DNA Polymerase γ Enhances DNA Binding, Promotes Processive DNA Synthesis, and Confers N-Ethylmaleimide Resistance
Lim, S. E., Longley, M. J., & Copeland, W. C. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.38197 · Cited by 226
Mitochondrial DNA mutations in human degenerative diseases and aging
Wallace, D. C., Shoffner, J. M., Trounce, I. A., Brown, M. D., Ballinger, S. W., Corral‐Debrinski, M., Horton, T. M., Jun, A. S., & Lott, M. T. (1995) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/0925-4439(95)00021-u · Cited by 225
Regulation of mitochondrial D‐loops by transcription factor A and single‐stranded DNA‐binding protein
Takamatsu, C., Umeda, S., Ohsato, T., Ohno, T., Abe, Y., Fukuoh, A., Shinagawa, H., Hamasaki, N., & Kang, D. (2002) · EMBO Reports · doi:10.1093/embo-reports/kvf099 · Cited by 220
Mammalian Mitochondrial DNA Replicates Bidirectionally from an Initiation Zone
Bowmaker, M., Yang, M., Yasukawa, T., Reyes, A., Jacobs, H. T., Huberman, J. A., & Holt, I. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m308028200 · Cited by 218
Human mitochondrial topoisomerase I
Zhang, H., Barceló, J. M., Lee, B., Kohlhagen, G., Zimonjic, D. B., Popescu, N. C., & Pommier, Y. G. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.191321998 · Cited by 215
Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates.
Huber, H. E., Tabor, S., & Richardson, C. C. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47719-8 · Cited by 210
Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius
Hopfner, K., Eichinger, A., Engh, R. A., Laue, F., Ankenbauer, W., Huber, R., & Angerer, B. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3600 · 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
Efficient Repair of Abasic Sites in DNA by Mitochondrial Enzymes
Pinz, K. G., & Bogenhagen, D. F. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1257 · Cited by 194
In vivo functional analysis of the human mitochondrial DNA polymerase POLG expressed in cultured human cells
Spelbrink, J. N., Toivonen, J. M., Hakkaart, G. A. J., Kurkela, J. M., Cooper, H. M., Lehtinen, S. K., Lecrenier, N., Back, J. W., Speijer, D., Foury, F., et al. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000559200 · Cited by 193
Side chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli.
Polesky, A. H., Dahlberg, M. E., Benkovic, S. J., Grindley, N. D. F., & Joyce, C. M. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42461-1 · Cited by 191
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
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
The mutational specificity of DNA polymerases-alpha and -gamma during in vitro DNA synthesis.
Kunkel, T. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)38958-5 · Cited by 176
Characterization of the Native and Recombinant Catalytic Subunit of Human DNA Polymerase γ: Identification of Residues Critical for Exonuclease Activity and Dideoxynucleotide Sensitivity
Longley, M. J., Ropp, P. A., Lim, S. E., & Copeland, W. C. (1998) · Biochemistry · doi:10.1021/bi980772w · Cited by 174
Novel 8-base pair sequence (Drosophila DNA replication-related element) and specific binding factor involved in the expression of Drosophila genes for DNA polymerase alpha and proliferating cell nuclear antigen.
Hirose, F., Yamaguchi, M., Handa, H., Inomata, Y., & Matsukage, A. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53966-1 · Cited by 170
Exonucleolytic proofreading enhances the fidelity of DNA synthesis by chick embryo DNA polymerase-gamma.
Kunkel, T. A., & Soni, A. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68947-1 · Cited by 167
Mitochondrial DNA depletion
Mancuso, M., Salviati, L., Sacconi, S., Otaegui, D., Camaño, P., Marina, A., Bacman, S. R., Moraes, C. T., Carlo, J., García, M. J., et al. (2002) · Neurology · doi:10.1212/01.wnl.0000028689.93049.9a · Cited by 167
Mitochondrial DNA depletion and dGK gene mutations
Salviati, L., Sacconi, S., Mancuso, M., Otaegui, D., Camaño, P., Marina, A., Rabinowitz, S. S., Shiffman, R. L., Thompson, K., Wilson, C. M., et al. (2002) · Annals of Neurology · doi:10.1002/ana.10284 · Cited by 161
Active Site Mutation in DNA Polymerase γ Associated with Progressive External Ophthalmoplegia Causes Error-prone DNA Synthesis
Ponamarev, M. V., Longley, M. J., Nguyen, D., Kunkel, T. A., & Copeland, W. C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200100200 · Cited by 156
Cardiac mitochondrial DNA polymerase-gamma is inhibited competitively and noncompetitively by phosphorylated zidovudine.
Lewis, W., Simpson, J. F., & Meyer, R. R. (1994) · Circulation Research · doi:10.1161/01.res.74.2.344 · Cited by 155
Repair of mtDNA in Vertebrates
Bogenhagen, D. F. (1999) · The American Journal of Human Genetics · doi:10.1086/302392 · Cited by 154
A New Synthetic RNA-Dependent DNA Polymerase from Human Tissue Culture Cells
Fridlender, B. R., Fry, M., Bolden, A. H., & Weissbach, A. (1972) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.69.2.452 · Cited by 152
Crystal Structure and Deletion Analysis Show that the Accessory Subunit of Mammalian DNA Polymerase γ, PolγB, Functions as a Homodimer
Carrodeguas, J. A., Theis, K., Bogenhagen, D. F., & Kisker, C. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00153-8 · Cited by 150
Human Mitochondrial DNA Polymerase Holoenzyme: Reconstitution and Characterization
Johnson, A. A., Tsai, Y., Graves, S. W., & Johnson, K. A. (2000) · Biochemistry · doi:10.1021/bi992104w · Cited by 147
Exonuclease Proofreading by Human Mitochondrial DNA Polymerase
Johnson, A. A., & Johnson, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106046200 · Cited by 141
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
Yeast mitochondrial DNA mutators with deficient proofreading exonucleolytic activity.
Foury, F., & Vanderstraeten, S. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05337.x · Cited by 138
Crystal structure of a pol α family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp . 9°N-7 1 1Edited by D. Rees
Rodriguez, A. C., Park, H.-W., Mao, C., & Beese, L. S. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.3728 · Cited by 137
A mitochondrial DNA polymerase from embryos of Drosophila melanogaster. Purification, subunit structure, and partial characterization.
Wernette, C. M., & Kaguni, L. S. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)66938-8 · Cited by 136
The mitochondrial DNA replication bubble has not burst
Bogenhagen, D. F., & Clayton, D. A. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00132-4 · Cited by 134
Insights into the Molecular Mechanism of Mitochondrial Toxicity by AIDS Drugs
Feng, J. Y., Johnson, A. A., Johnson, K. A., & Anderson, K. S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101156200 · Cited by 130
A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
Carroll, S. S., Cowart, M., & Benkovic, S. J. (1991) · Biochemistry · doi:10.1021/bi00217a034 · Cited by 125
Construction of transgenic mice with tissue-specific acceleration of mitochondrial DNA mutagenesis
Zhang, D., Mott, J. L., Chang, S.-W., Denniger, G., Feng, Z., & Zassenhaus, H. P. (2000) · Genomics · doi:10.1006/geno.2000.6333 · Cited by 124
Action of Mitochondrial DNA Polymerase γ at Sites of Base Loss or Oxidative Damage
Pinz, K. G., Shibutani, S., & Bogenhagen, D. F. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.16.9202 · Cited by 123
Fidelity of Nucleotide Incorporation by Human Mitochondrial DNA Polymerase
Johnson, A. A., & Johnson, K. A. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106045200 · Cited by 122
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
Mitochondrial DNA mutations activate the mitochondrial apoptotic pathway and cause dilated cardiomyopathy
Zhang, D. (2003) · Cardiovascular Research · doi:10.1016/s0008-6363(02)00695-8 · Cited by 115
Deoxynucleoside Triphosphate and Pyrophosphate Binding Sites in the Catalytically Competent Ternary Complex for the Polymerase Reaction Catalyzed by DNA Polymerase I (Klenow Fragment)
Astatke, M., Grindley, N. D. F., & Joyce, C. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.4.1945 · Cited by 112
How E. coli DNA polymerase I (klenow fragment) distinguishes between deoxy- and dideoxynucleotides
Astatke, M., Grindley, N. D. F., & Joyce, C. M. (1998) · Journal of Molecular Biology · doi:10.1006/jmbi.1998.1672 · Cited by 109
Functional Interactions of Mitochondrial DNA Polymerase and Single-stranded DNA-binding Protein
Farr, C. L., Wang, Y., & Kaguni, L. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.21.14779 · Cited by 108
The Accessory Subunit of Xenopus laevis Mitochondrial DNA Polymerase γ Increases Processivity of the Catalytic Subunit of Human DNA Polymerase γ and Is Related to Class II Aminoacyl-tRNA Synthetases
Carrodeguas, J. A., Kobayashi, R., Lim, S. E., Copeland, W. C., & Bogenhagen, D. F. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4039 · Cited by 108
The functional roles of mammalian DNA polymerase
Weissbach, A. (1979) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(79)90511-3 · Cited by 105
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
A deoxyribonucleotidase in mitochondria: Involvement in regulation of dNTP pools and possible link to genetic disease
Rampazzo, C., Gallinaro, L., Milanesi, E., Frigimelica, E., Reichard, P. A., & Bianchi, V. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.15.8239 · Cited by 96
The Role of 3′-5′ Exonucleolytic Proofreading and Mismatch Repair in Yeast Mitochondrial DNA Error Avoidance
Vanderstraeten, S., van den Brûle, S., Hu, J., & Foury, F. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.37.23690 · Cited by 91
DNA Polymerase Gamma in Mitochondrial DNA Replication and Repair
Copeland, W. C., & Longley, M. J. (2003) · The Scientific World JOURNAL · doi:10.1100/tsw.2003.09 · Cited by 91
Nuclear genes in mitochondrial disorders
Zeviani, M., Spinazzola, A., & Carelli, V. (2003) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(03)00052-2 · Cited by 89
The DNA Replication-related Element (DRE)/DRE-binding Factor System Is a Transcriptional Regulator of the Drosophila E2FGene
Sawado, T., Hirose, F., Takahashi, Y., Sasaki, T., Shinomiya, T., Sakaguchi, K., Matsukage, A., & Yamaguchi, M. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.40.26042 · Cited by 89
The accessory subunit of mtDNA polymerase shares structural homology with aminoacyl-tRNA synthetases: Implications for a dual role as a primer recognition factor and processivity clamp
Fan, L., Sanschagrin, P. C., Kaguni, L. S., & Kuhn, L. A. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.17.9527 · Cited by 89
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
DNA polymerase γ from Xenopus laevis
Insdorf, N. F., & Bogenhagen, D. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88211-8 · Cited by 86
Structural Determinants in Human DNA Polymerase γ Account for Mitochondrial Toxicity from Nucleoside Analogs
Lim, S. E., Ponamarev, M. V., Longley, M. J., & Copeland, W. C. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00405-4 · Cited by 85
Mitochondrial Single-stranded DNA-binding Protein Is Required for Mitochondrial DNA Replication and Development inDrosophila melanogaster
Maier, D., Farr, C. L., Poeck, B., Alahari, A., Vogel, M. J., Fischer, S., Kaguni, L. S., & Schneuwly, S. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.4.821 · Cited by 82
Characterization of a Catalytically Slow AP Lyase Activity in DNA Polymerase γ and Other Family A DNA Polymerases
Pinz, K. G., & Bogenhagen, D. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12509 · Cited by 81
Antisense-mediated decrease in DNA ligase III expression results in reduced mitochondrial DNA integrity
Lakshmipathy, U. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.3.668 · Cited by 81
Chick embryo DNA polymerase gamma. Purification and structural analysis of nearly homogeneous enzyme.
Yamaguchi, M., Matsukage, A., & Takahashi, T. (1980) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43675-7 · Cited by 78
RNA- and single-stranded DNA-binding (SSB) proteins expressed during Drosophila melanogaster oogenesis: a homolog of bacterial and eukaryotic mitochondrial SSBs
Stroumbakis, N. D., Li, Z., & Tolias, P. P. (1994) · Gene · doi:10.1016/0378-1119(94)90093-0 · Cited by 78
Base Miscoding and Strand Misalignment Errors by Mutator Klenow Polymerases with Amino Acid Substitutions at Tyrosine 766 in the O Helix of the Fingers Subdomain
Bell, J. B., Eckert, K. A., Joyce, C. M., & Kunkel, T. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.11.7345 · Cited by 76
Isolation and characterization of a DNA primase from human mitochondria.
Wong, T. W., & Clayton, D. A. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39063-4 · Cited by 75
Response: The mitochondrial DNA replication bubble has not burst
Holt, I. J., & Jacobs, H. T. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00133-6 · Cited by 75
Transcriptional regulation of the Drosophila CycA gene by the DNA replication-related element (DRE) and DRE binding factor (DREF)
Ohno, K. (1996) · Nucleic Acids Research · doi:10.1093/nar/24.20.3942 · Cited by 74
The tamas Gene, Identified as a Mutation That Disrupts Larval Behavior in Drosophila melanogaster, Codes for the Mitochondrial DNA Polymerase Catalytic Subunit (DNApol-γ125)
Iyengar, B. G., Roote, J., & Campos, A. R. (1999) · Genetics · doi:10.1093/genetics/153.4.1809 · Cited by 72
Exonucleolytic proofreading by a mammalian DNA polymerase .gamma.
Kunkel, T. A., & Mosbaugh, D. W. (1989) · Biochemistry · doi:10.1021/bi00429a011 · Cited by 71
Accessory Subunit of Mitochondrial DNA Polymerase fromDrosophila Embryos
Wang, Y., Farr, C. L., & Kaguni, L. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.21.13640 · Cited by 70
Genetic and biochemical studies of bacteriophage T4 DNA polymerase 3'-->5'-exonuclease activity.
Reha-Krantz, L. J., & Nonay, R. L. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74223-9 · Cited by 69
Yeast mitochondrial RNA polymerase. Purification and properties of the catalytic subunit.
Kelly, J. L., & Lehman, I. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67529-5 · Cited by 67
The rat liver mitochondrial DNA-protein complex: displaced single strands of replicative intermediates are protein coated.
Tuyle, G. C. V., & Pavco, P. A. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.251 · Cited by 67
Characterization of a mitochondrial protein binding to single-stranded DNA
Mignotte, B., Barat, M., & Mounolou, J. (1985) · Nucleic Acids Research · doi:10.1093/nar/13.5.1703 · Cited by 63
A nuclear mutant of Saccharomyces cerevisiae deficient in mitochondrial DNA replication and polymerase activity.
Genga, A., Bianchi, L., & Foury, F. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)67658-6 · Cited by 62
DNA Binding Properties of Human pol γB
Carrodeguas, J. A., Pinz, K. G., & Bogenhagen, D. F. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207030200 · Cited by 59
Yeast as a Model for Human mtDNA Replication
Shadel, G. S. (1999) · The American Journal of Human Genetics · doi:10.1086/302630 · Cited by 58
DNA Replication-related Elements Cooperate to Enhance Promoter Activity of the DNA Polymerase α 73-kDa Subunit Gene
Takahashi, Y., Yamaguchi, M., Hirose, F., Cotterill, S., Kobayashi, J., Miyajima, S., & Matsukage, A. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.24.14541 · Cited by 55
Unusual compartmentation of precursors for nuclear and mitochondrial DNA in mouse L cells.
Bestwick, R. K., & Mathews, C. K. (1982) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)34069-9 · Cited by 53
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
The accessory subunit of DNA polymerase γ is essential for mitochondrial DNA maintenance and development in Drosophila melanogaster
Iyengar, B. G., Luo, N., Farr, C. L., Kaguni, L. S., & Campos, A. R. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.072664899 · Cited by 53
Properties of the 3‘ to 5‘ exonuclease associated with porcine liver DNA polymerase gamma. Substrate specificity, product analysis, inhibition, and kinetics of terminal excision.
Longley, M. J., & Mosbaugh, D. W. (1991) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)54287-3 · Cited by 52
Catalytic Subunit of Mitochondrial DNA Polymerase from Embryos
Lewis, D. L., Farr, C. L., Wang, Y., Lagina, A. T., & Kaguni, L. S. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.38.23389 · Cited by 52
Mitochondrial Single-stranded DNA-binding Protein from Drosophila Embryos
Thommes, P. A., Farr, C. L., Marton, R. F., Kaguni, L. S., & Cotterill, S. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.36.21137 · Cited by 51
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
Yeast mitochondrial DNA polymerase is related to the family A DNA polymerases
Ito, J., & Braithwaite, D. K. (1990) · Nucleic Acids Research · doi:10.1093/nar/18.22.6716 · Cited by 48
Characterization of Novel Reverse Transcriptase and Other RNA-associated Catalytic Activities by Human DNA Polymerase γ
Murakami, E., Feng, J. Y., Lee, H., Hanes, J. W., Johnson, K. A., & Anderson, K. S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306236200 · Cited by 47
DNA polymerase γ from Xenopus laevis
Insdorf, N. F., & Bogenhagen, D. F. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(20)88212-x · Cited by 45
Purification and general properties of the DNA-binding protein (P16) from rat liver mitochondria.
Pavco, P. A., & Tuyle, G. C. V. (1985) · The Journal of Cell Biology · doi:10.1083/jcb.100.1.258 · Cited by 45
Concluding remarks: The mitochondrial DNA replication bubble has not burst
Bogenhagen, D. F., & Clayton, D. A. (2003) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(03)00165-8 · Cited by 45
Isolation and characterization of ten mutator alleles of the mitochondrial DNA polymerase-encoding MIP1 gene from Saccharomyces cerevisiae
Hu, J., Vanderstraeten, S., & Foury, F. (1995) · Gene · doi:10.1016/0378-1119(95)00215-r · Cited by 45
Mismatch-specific 3'----5' exonuclease associated with the mitochondrial DNA polymerase from Drosophila embryos.
Kaguni, L. S., & Olson, M. W. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6469 · Cited by 44
3‘–>5‘ exonuclease in Drosophila mitochondrial DNA polymerase. Substrate specificity and functional coordination of nucleotide polymerization and mispair hydrolysis
Olson, M. W., & Kaguni, L. S. (1992) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)50067-3 · Cited by 43
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
Mitochondrial DNA polymerase from Drosophila melanogaster embryos: kinetics, processivity, and fidelity of DNA polymerization
Wernette, C. M., Conway, M. C., & Kaguni, L. S. (1988) · Biochemistry · doi:10.1021/bi00416a033 · Cited by 42
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
Overexpression of the RNR1 gene rescues Saccharomyces cerevisiae mutants in the mitochondrial DNA polymerase-encoding MIP1 gene
Lecrenier, N., & Foury, F. (1995) · Molecular and General Genetics MGG · doi:10.1007/bf00290229 · Cited by 39
Regulation of Mitochondrial Single-stranded DNA-binding Protein Gene Expression Links Nuclear and Mitochondrial DNA Replication inDrosophila
de Mena, I. R., Lefai, É., Garesse, R., & Kaguni, L. S. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.18.13628 · Cited by 39
Tetramerization and Single-stranded DNA Binding Properties of Native and Mutated Forms of Murine Mitochondrial Single-stranded DNA-binding Proteins
Li, K., & Williams, R. S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.13.8686 · Cited by 39
Differential Regulation of the Catalytic and Accessory Subunit Genes of Drosophila Mitochondrial DNA Polymerase
Lefai, É., Fernández‐Moreno, M. Á., Alahari, A., Kaguni, L. S., & Garesse, R. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003024200 · Cited by 36
A full-length cDNA encoding a mitochondrial DNA-specific single-stranded DNA binding protein fromXenopus laevis
Tiranti, V., Guéride, M., Bijl, J. J., DiDonato, S., & Zeviani, M. (1991) · Nucleic Acids Research · doi:10.1093/nar/19.15.4291 · Cited by 35
Overexpression of the catalytic subunit of DNA polymerase γ results in depletion of mitochondrial DNA in Drosophila melanogaster
Lefai, É., Calleja, M., de Mena, I. R., Lagina, A. T., Kaguni, L. S., & Garesse, R. (2000) · Molecular and General Genetics MGG · doi:10.1007/s004380000301 · Cited by 34
Effects of the Xenopus laevis mitochondrial single‐stranded DNA‐binding protein on the activity of DNA polymerase γ
Mignotte, B., Marsault, J., & BARAT‐GUERIDE, M. (1988) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1988.tb14123.x · Cited by 33
Characterization of a rat liver mitochondrial DNA-protein complex. Replicative intermediates are protected against branch migrational loss.
Tuyle, G. C. V., & Pavco, P. A. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)42962-6 · Cited by 31
Processivity of mitochondrial DNA polymerase from Drosophila embryos. Effects of reaction conditions and enzyme purity.
Williams, A. J., Wernette, C. M., & Kaguni, L. S. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74543-8 · Cited by 30
Effects of Xenopus laevis Mitochondrial Single-stranded DNA-binding Protein on Primer-Template Binding and 3′→5′ Exonuclease Activity of DNA Polymerase γ
Mikhailov, V. S., & Bogenhagen, D. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.31.18939 · Cited by 30
Primary structure of the two variants of Xenopus laevis mtSSB, a mitochondrial DNA binding protein
Ghrir, R., Caër, J. L., Dufresne, C., & Guéride, M. (1991) · Archives of Biochemistry and Biophysics · doi:10.1016/0003-9861(91)90152-9 · Cited by 30
Two Forms of Mitochondrial DNA Ligase III Are Produced inXenopus laevis Oocytes
Perez-Jannotti, R. M., Klein, S. M., & Bogenhagen, D. F. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m107177200 · Cited by 29
Characterization of a new DNA polymerase from Schizosaccharomyces pombe: a probable homologue of the Saccharomyces cerevisiae DNA polymerase gamma
Ropp, P. A., & Copeland, W. C. (1995) · Gene · doi:10.1016/0378-1119(95)00412-y · Cited by 28
Multiple Regions of Subunit Interaction in Drosophila Mitochondrial DNA Polymerase: Three Functional Domains in the Accessory Subunit
Fan, L., & Kaguni, L. S. (2001) · Biochemistry · doi:10.1021/bi010102h · Cited by 26
Termination within Oligo(dT) Tracts in Template DNA by DNA Polymerase γ Occurs with Formation of a DNA Triplex Structure and Is Relieved by Mitochondrial Single-stranded DNA-binding Protein
Mikhailov, V. S., & Bogenhagen, D. F. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.48.30774 · Cited by 24
Baculovirus Expression Reconstitutes DrosophilaMitochondrial DNA Polymerase
Wang, Y., & Kaguni, L. S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.41.28972 · Cited by 24
Low Frequencies of Mitochondrial DNA Mutations Cause Cardiac Disease in the Mouse
Mott, J. L., Zhang, D., Farrar, P. L., Chang, S.-J., & Zassenhaus, H. P. (1999) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.1999.tb07853.x · Cited by 17
The highly compact structure of the mitochondrial DNA polymerase genomic region of Drosophila melanogaster : functional and evolutionary implications
Lefai, É., Fernández‐Moreno, M. Á., Kaguni, L. S., & Garesse, R. (2000) · Insect Molecular Biology · doi:10.1046/j.1365-2583.2000.00191.x · Cited by 11

Research works printed but not linked: 4

Kaguni LS, Wernette CM, Conway MC, Yang-Cashman P. 1988. In Cancer Cells: Eukaryotic DNA Replication , ed. TJ Kelly, B Stillman, pp. 425–32. Cold Spring Harbor, NY: Cold Spring Harbor Lab.
Farr CL, 2004, J. Biol. Chem.
Kornberg A, 1992, DNA Replication.
Genuario R, 1993, Cell. Mol. Biol. Res., 39, 625

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Authors: Kaguni, L. S.
Affiliations: Michigan State University (US)
Corresponding author: Kaguni, Laurie S.
Venue: Annual Review of Biochemistry
Publisher: Annual Reviews
Published: 2004-06
Volume: 73
Issue: 1
Pages: 293-320
ISSN: 0066-4154 (ISSN-L)
1545-4509
DOI: 10.1146/annurev.biochem.72.121801.161455
OpenAlex: W2128968369
Cited by: 414
References: 156
Citations by year: 2026: 8 · 2025: 13 · 2024: 11 · 2023: 12 · 2022: 13 · 2021: 12 · 2020: 15 · 2019: 10 · 2018: 11 · 2017: 16 · 2016: 23 · 2015: 16 · 2014: 16 · 2013: 21 · 2012: 26
FWCI: 1.40
Type: journal article
Language: en
Open access: closed
Locations: Annual Review of Biochemistry (publishedVersion)
PubMed (publishedVersion)
Funders: American Cancer Society
National Institutes of Health (5r01hl059656-03, 5r01gm034042-03)
National Heart, Lung, and Blood Institute (HL59656)
National Institute of General Medical Sciences (R01GM045295, GM34042, GM45295)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA and Nucleic Acid Chemistry
Keywords: DNA polymerase gamma, mitochondrial DNA replication, mitochondrial DNA repair, DNA recombination, nucleotide misincorporation, mitochondrial mutagenesis, mitochondrial dysfunction
MeSH terms: DNA Polymerase gamma, Amino Acid Sequence, Animals, DNA-Directed DNA Polymerase, DNA Replication, Exonucleases, Humans, Mitochondria, Models, Molecular, Molecular Sequence Data, Mutagenesis, Sequence Homology, Amino Acid, Protein Subunits, History, 20th Century

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DNA Polymerase γ, The Mitochondrial Replicase

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