메뉴 건너뛰기




Volumn 22, Issue 5, 2004, Pages 253-260

Recent developments in the optimization of thermostable DNA polymerases for efficient applications

Author keywords

[No Author keywords available]

Indexed keywords

DNA; ENZYMES; GENETIC ENGINEERING; OPTIMIZATION;

EID: 1942534174     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2004.02.011     Document Type: Review
Times cited : (87)

References (94)
  • 1
    • 0017108645 scopus 로고
    • Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus
    • Chien A., et al. Deoxyribonucleic acid polymerase from the extreme thermophile Thermus aquaticus. J. Bacteriol. 127:1976;1550-1557.
    • (1976) J. Bacteriol. , vol.127 , pp. 1550-1557
    • Chien, A.1
  • 2
    • 0019002898 scopus 로고
    • Isolation and properties of DNA polymerase from extreme thermophylic bacteria Thermus aquaticus YT-1
    • Kaledin A.S., et al. Isolation and properties of DNA polymerase from extreme thermophylic bacteria Thermus aquaticus YT-1. Biokhimiia. 45:1980;644-651.
    • (1980) Biokhimiia , vol.45 , pp. 644-651
    • Kaledin, A.S.1
  • 3
    • 0022372670 scopus 로고
    • Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia
    • Saiki R.K., et al. Enzymatic amplification of β-globin genomic sequences and restriction site analysis for diagnosis of sickle cell anemia. Science. 230:1985;1350-1354.
    • (1985) Science , vol.230 , pp. 1350-1354
    • Saiki, R.K.1
  • 4
    • 0001040973 scopus 로고
    • DNA sequencing with Thermus aquaticus DNA polymerase and direct sequencing of polymerase chain reaction-amplified DNA
    • Innis M.A., et al. DNA sequencing with Thermus aquaticus DNA polymerase and direct sequencing of polymerase chain reaction-amplified DNA. Proc. Natl. Acad. Sci. U. S. A. 85:1988;9436-9440.
    • (1988) Proc. Natl. Acad. Sci. U. S. A. , vol.85 , pp. 9436-9440
    • Innis, M.A.1
  • 5
    • 0028983795 scopus 로고
    • Crystal structure of Thermus aquaticus DNA polymerase
    • Kim Y., et al. Crystal structure of Thermus aquaticus DNA polymerase. Nature. 376:1995;612-616.
    • (1995) Nature , vol.376 , pp. 612-616
    • Kim, Y.1
  • 6
    • 0033570179 scopus 로고    scopus 로고
    • Crystal structure of an archaebacterial DNA polymerase
    • Zhao Y., et al. Crystal structure of an archaebacterial DNA polymerase. Structure Fold. Des. 7:1999;1189-1199.
    • (1999) Structure Fold. Des. , vol.7 , pp. 1189-1199
    • Zhao, Y.1
  • 7
    • 0035936690 scopus 로고    scopus 로고
    • Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1
    • Hashimoto H., et al. Crystal structure of DNA polymerase from hyperthermophilic archaeon Pyrococcus kodakaraensis KOD1. J. Mol. Biol. 306:2001;469-477.
    • (2001) J. Mol. Biol. , vol.306 , pp. 469-477
    • Hashimoto, H.1
  • 8
    • 0033616725 scopus 로고    scopus 로고
    • Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius
    • Hopfner K.-P., et al. Crystal structure of a thermostable type B DNA polymerase from Thermococcus gorgonarius. Proc. Natl. Acad. Sci. U. S. A. 96:1999;3600-3605.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 3600-3605
    • Hopfner, K.-P.1
  • 9
    • 0031922356 scopus 로고    scopus 로고
    • A novel DNA polymerase family found in archaea
    • Ishino Y., et al. A novel DNA polymerase family found in archaea. J. Bacteriol. 180:1998;2232-2236.
    • (1998) J. Bacteriol. , vol.180 , pp. 2232-2236
    • Ishino, Y.1
  • 10
    • 0037079680 scopus 로고    scopus 로고
    • A DNA repair system specific for thermophilic archaea and bacteria predicted by genomic context analysis
    • Makarova K.S., et al. A DNA repair system specific for thermophilic archaea and bacteria predicted by genomic context analysis. Nucleic Acids Res. 30:2002;482-496.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 482-496
    • Makarova, K.S.1
  • 12
    • 0025766848 scopus 로고
    • Compilation and alignment of DNA polymerase sequences
    • Ito J., Braithwaite D.K. Compilation and alignment of DNA polymerase sequences. Nucleic Acids Res. 19:1991;4045-4057.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4045-4057
    • Ito, J.1    Braithwaite, D.K.2
  • 13
    • 0032814005 scopus 로고    scopus 로고
    • Archaeal DNA replication: Identifying the pieces to solve a puzzle
    • Cann I.K.O., Ishino Y. Archaeal DNA replication: identifying the pieces to solve a puzzle. Genetics. 152:1999;1249-1267.
    • (1999) Genetics , vol.152 , pp. 1249-1267
    • Cann, I.K.O.1    Ishino, Y.2
  • 14
    • 17944380943 scopus 로고    scopus 로고
    • The Y-family of DNA polymerases
    • Ohmori H., et al. The Y-family of DNA polymerases. Mol. Cell. 8:2001;7-8.
    • (2001) Mol. Cell , vol.8 , pp. 7-8
    • Ohmori, H.1
  • 15
    • 0028606031 scopus 로고
    • A unified polymerase mechanism for nonhomologous DNA and RNA polymerases
    • Steitz T.A., et al. A unified polymerase mechanism for nonhomologous DNA and RNA polymerases. Science. 266:1994;2022-2025.
    • (1994) Science , vol.266 , pp. 2022-2025
    • Steitz, T.A.1
  • 16
    • 0030909129 scopus 로고    scopus 로고
    • Genetic information 'created' by archaebacterial DNA polymerase
    • Ogata N., Miura T. Genetic information 'created' by archaebacterial DNA polymerase. Biochem. J. 324:1997;667-671.
    • (1997) Biochem. J. , vol.324 , pp. 667-671
    • Ogata, N.1    Miura, T.2
  • 17
    • 0032531867 scopus 로고    scopus 로고
    • Creation of genetic information by DNA polymerase of the archaeon Thermococcus litoralis: Influences of temperature and ionic strength
    • Ogata N., Miura T. Creation of genetic information by DNA polymerase of the archaeon Thermococcus litoralis: influences of temperature and ionic strength. Nucleic Acids Res. 26:1998;4652-4656.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4652-4656
    • Ogata, N.1    Miura, T.2
  • 18
    • 0032531739 scopus 로고    scopus 로고
    • Creation of genetic information by DNA polymerase of the thermophilic bacterium Thermus thermophilus
    • Ogata N., Miura T. Creation of genetic information by DNA polymerase of the thermophilic bacterium Thermus thermophilus. Nucleic Acids Res. 26:1998;4657-4661.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4657-4661
    • Ogata, N.1    Miura, T.2
  • 19
    • 0032489234 scopus 로고    scopus 로고
    • Two different reactions involved in the primer/template-independent polymerization of dATP and dTTP by Taq DNA polymerase
    • Hanaki K., et al. Two different reactions involved in the primer/template-independent polymerization of dATP and dTTP by Taq DNA polymerase. Biochem. Biophys. Res. Commun. 244:1998;210-219.
    • (1998) Biochem. Biophys. Res. Commun. , vol.244 , pp. 210-219
    • Hanaki, K.1
  • 20
    • 0027215222 scopus 로고
    • Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases
    • Lyamichev V., et al. Structure-specific endonucleolytic cleavage of nucleic acids by eubacterial DNA polymerases. Science. 260:1993;778-783.
    • (1993) Science , vol.260 , pp. 778-783
    • Lyamichev, V.1
  • 21
    • 0026631716 scopus 로고
    • Increased thermal stability of proteins in the presence of naturally occurring osmolytes
    • Santoro M.M., et al. Increased thermal stability of proteins in the presence of naturally occurring osmolytes. Biochemistry. 31:1992;5278-5283.
    • (1992) Biochemistry , vol.31 , pp. 5278-5283
    • Santoro, M.M.1
  • 22
    • 0037109049 scopus 로고    scopus 로고
    • Helix-hairpin-helix motifs confer salt resistance and processivity on chimeric DNA polymerases
    • Pavlov A.R., et al. Helix-hairpin-helix motifs confer salt resistance and processivity on chimeric DNA polymerases. Proc. Natl. Acad. Sci. U. S. A. 99:2002;13510-13515.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 13510-13515
    • Pavlov, A.R.1
  • 23
    • 0037308304 scopus 로고    scopus 로고
    • Effects of types of sugar on the stabilization of protein in the dried state
    • Imamura K., et al. Effects of types of sugar on the stabilization of protein in the dried state. J. Pharm. Sci. 92:2003;266-274.
    • (2003) J. Pharm. Sci. , vol.92 , pp. 266-274
    • Imamura, K.1
  • 24
    • 0020953558 scopus 로고
    • On the processivity of DNA replication
    • Fairfield F.R., et al. On the processivity of DNA replication. J. Biomol. Struct. Dyn. 1:1983;715-727.
    • (1983) J. Biomol. Struct. Dyn. , vol.1 , pp. 715-727
    • Fairfield, F.R.1
  • 25
    • 0027940241 scopus 로고
    • On the processivity of polymerases
    • von Hippel P.H., et al. On the processivity of polymerases. Ann. N. Y. Acad. Sci. 726:1994;118-131.
    • (1994) Ann. N. Y. Acad. Sci. , vol.726 , pp. 118-131
    • Von Hippel, P.H.1
  • 26
    • 0033601194 scopus 로고    scopus 로고
    • Fidelity and processivity of Saccharomyces cerevisiae DNA poymerase η
    • Washington M.T., et al. Fidelity and processivity of Saccharomyces cerevisiae DNA poymerase η J. Biol. Chem. 274:1999;36835-36838.
    • (1999) J. Biol. Chem. , vol.274 , pp. 36835-36838
    • Washington, M.T.1
  • 27
    • 0037032998 scopus 로고    scopus 로고
    • Efficiency of correct nucleotide insertion governs DNA polymerase fidelity
    • Beard W.A., et al. Efficiency of correct nucleotide insertion governs DNA polymerase fidelity. J. Biol. Chem. 277:2002;47393-47398.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47393-47398
    • Beard, W.A.1
  • 28
    • 0037566670 scopus 로고    scopus 로고
    • Structural insights into the origins of DNA polymerase fidelity
    • Beard W.A., Wilson S.H. Structural insights into the origins of DNA polymerase fidelity. Structure Fold. Des. 11:2003;489-496.
    • (2003) Structure Fold. Des. , vol.11 , pp. 489-496
    • Beard, W.A.1    Wilson, S.H.2
  • 29
    • 0026207466 scopus 로고
    • DNA polymerase fidelity and the polymerase chain reaction
    • Eckert K.A., Kunkel T.A. DNA polymerase fidelity and the polymerase chain reaction. PCR Methods Appl. 1:1991;17-24.
    • (1991) PCR Methods Appl. , vol.1 , pp. 17-24
    • Eckert, K.A.1    Kunkel, T.A.2
  • 30
    • 0024282746 scopus 로고
    • Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase
    • Tindall K.R., Kunkel T.A. Fidelity of DNA synthesis by the Thermus aquaticus DNA polymerase. Biochemistry. 27:1988;6008-6013.
    • (1988) Biochemistry , vol.27 , pp. 6008-6013
    • Tindall, K.R.1    Kunkel, T.A.2
  • 31
    • 0030807050 scopus 로고    scopus 로고
    • A coalescent approach to the polymerase chain reaction
    • Weiss G., von Haeseler A. A coalescent approach to the polymerase chain reaction. Nucleic Acids Res. 25:1997;3082-3087.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3082-3087
    • Weiss, G.1    Von Haeseler, A.2
  • 32
    • 0034100229 scopus 로고    scopus 로고
    • Estimation of the mutation rate during error-prone polymerase chain reaction
    • Wang D., et al. Estimation of the mutation rate during error-prone polymerase chain reaction. J. Comput. Biol. 7:2000;143-158.
    • (2000) J. Comput. Biol. , vol.7 , pp. 143-158
    • Wang, D.1
  • 33
    • 0026534432 scopus 로고
    • The fidelity of Taq polymerase catalyzing PCR is improved by an N-terminal deletion
    • Barnes W.M. The fidelity of Taq polymerase catalyzing PCR is improved by an N-terminal deletion. Gene. 112:1992;29-35.
    • (1992) Gene , vol.112 , pp. 29-35
    • Barnes, W.M.1
  • 34
    • 0029981239 scopus 로고    scopus 로고
    • Heterogeneity of primer extension products in asymmetric PCR is due both to cleavage by a structure-specific exo/endonuclease activity of DNA polymerases and to premature stops
    • Tombline G., et al. Heterogeneity of primer extension products in asymmetric PCR is due both to cleavage by a structure-specific exo/endonuclease activity of DNA polymerases and to premature stops. Proc. Natl. Acad. Sci. U. S. A. 93:1996;2724-2728.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 2724-2728
    • Tombline, G.1
  • 35
    • 0344011118 scopus 로고    scopus 로고
    • Cold-sensitive mutants of Taq DNA polymerase provide a hot start for PCR
    • Kermekchiev M.B., et al. Cold-sensitive mutants of Taq DNA polymerase provide a hot start for PCR. Nucleic Acids Res. 31:2003;6139-6147.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 6139-6147
    • Kermekchiev, M.B.1
  • 37
    • 0029023051 scopus 로고
    • A single residue in DNA polymerases of the Escherichia coli DNA polymerase I family is critical for distinguishing between deoxy- and dideoxyribonucleotides
    • Tabor S., Richardson C.C. A single residue in DNA polymerases of the Escherichia coli DNA polymerase I family is critical for distinguishing between deoxy- and dideoxyribonucleotides. Proc. Natl. Acad. Sci. U. S. A. 92:1995;6339-6343.
    • (1995) Proc. Natl. Acad. Sci. U. S. A. , vol.92 , pp. 6339-6343
    • Tabor, S.1    Richardson, C.C.2
  • 38
    • 0033578332 scopus 로고    scopus 로고
    • Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation
    • Li Y., et al. Structure-based design of Taq DNA polymerases with improved properties of dideoxynucleotide incorporation. Proc. Natl. Acad. Sci. U. S. A. 96:1999;9491-9496.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 9491-9496
    • Li, Y.1
  • 39
    • 0036799219 scopus 로고    scopus 로고
    • Mutant Thermotoga neapolitana DNA polymerase I: Altered catalytic properties for non-templated nucleotide addition and incorporation of correct nucleotides
    • Yang S.-W., et al. Mutant Thermotoga neapolitana DNA polymerase I: altered catalytic properties for non-templated nucleotide addition and incorporation of correct nucleotides. Nucleic Acids Res. 30:2002;4314-4320.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 4314-4320
    • Yang, S.-W.1
  • 40
    • 0034160088 scopus 로고    scopus 로고
    • Improving dideoxynucleotide-triphosphate utilisation by the hyper-thermophilic DNA polymerase from the archaeon Pyrococcus furiosus
    • Evans S.J., et al. Improving dideoxynucleotide-triphosphate utilisation by the hyper-thermophilic DNA polymerase from the archaeon Pyrococcus furiosus. Nucleic Acids Res. 28:2000;1059-1066.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 1059-1066
    • Evans, S.J.1
  • 41
    • 0033564079 scopus 로고    scopus 로고
    • Determinants of nucleotide sugar recognition in an archaeon DNA polymerase
    • Gardner A., Jack W. Determinants of nucleotide sugar recognition in an archaeon DNA polymerase. Nucleic Acids Res. 27:1999;2545-2553.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 2545-2553
    • Gardner, A.1    Jack, W.2
  • 42
    • 0037079661 scopus 로고    scopus 로고
    • Acyclic and dideoxy terminator preferences denote divergent sugar recognition by archaeon and Taq DNA polymerases
    • Gardner A.F., Jack W.E. Acyclic and dideoxy terminator preferences denote divergent sugar recognition by archaeon and Taq DNA polymerases. Nucleic Acids Res. 30:2002;605-613.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 605-613
    • Gardner, A.F.1    Jack, W.E.2
  • 43
    • 0036387195 scopus 로고    scopus 로고
    • Efficient and high fidelity incorporation of dye-terminators by a novel archaeal DNA polymerase mutant
    • Arezi B., et al. Efficient and high fidelity incorporation of dye-terminators by a novel archaeal DNA polymerase mutant. J. Mol. Biol. 322:2002;719-729.
    • (2002) J. Mol. Biol. , vol.322 , pp. 719-729
    • Arezi, B.1
  • 44
    • 0036897839 scopus 로고    scopus 로고
    • Milestones in directed enzyme evolution
    • Tao H., Cornish V.W. Milestones in directed enzyme evolution. Curr. Opin. Chem. Biol. 6:2002;858-864.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 858-864
    • Tao, H.1    Cornish, V.W.2
  • 45
    • 0035836707 scopus 로고    scopus 로고
    • Directed evolution of polymerase function by compartmentalized self-replication
    • Ghadessy F.J., et al. Directed evolution of polymerase function by compartmentalized self-replication. Proc. Natl. Acad. Sci. U. S. A. 98:2001;4552-4557.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 4552-4557
    • Ghadessy, F.J.1
  • 46
    • 0037076311 scopus 로고    scopus 로고
    • Directed evolution of novel polymerase activities: Mutation of a DNA polymerase into an efficient RNA polymerase
    • Xia G., et al. Directed evolution of novel polymerase activities: mutation of a DNA polymerase into an efficient RNA polymerase. Proc. Natl. Acad. Sci. U. S. A. 99:2002;6597-6602.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 6597-6602
    • Xia, G.1
  • 47
    • 0033776997 scopus 로고    scopus 로고
    • Domain exchange: Chimeras of Thermus aquaticus DNA polymerase, Escherichia coli DNA polymerase I and Thermotoga neapolitana DNA polymerase
    • Villbrandt B., et al. Domain exchange: chimeras of Thermus aquaticus DNA polymerase, Escherichia coli DNA polymerase I and Thermotoga neapolitana DNA polymerase. Protein Eng. 13:2000;645-654.
    • (2000) Protein Eng. , vol.13 , pp. 645-654
    • Villbrandt, B.1
  • 48
    • 0037013241 scopus 로고    scopus 로고
    • Elucidation of an archaeal replication protein network to generate enhanced PCR enzymes
    • Motz M., et al. Elucidation of an archaeal replication protein network to generate enhanced PCR enzymes. J. Biol. Chem. 277:2002;16179-16188.
    • (2002) J. Biol. Chem. , vol.277 , pp. 16179-16188
    • Motz, M.1
  • 49
    • 0344875539 scopus 로고    scopus 로고
    • Insertion of the T3 DNA polymerase thioredoxin binding domain enhances the processivity and fidelity of Taq DNA polymerase
    • Davidson J.F., et al. Insertion of the T3 DNA polymerase thioredoxin binding domain enhances the processivity and fidelity of Taq DNA polymerase. Nucleic Acids Res. 31:2003;4702-4709.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 4702-4709
    • Davidson, J.F.1
  • 50
    • 0031030318 scopus 로고    scopus 로고
    • The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I
    • Bedford E., et al. The thioredoxin binding domain of bacteriophage T7 DNA polymerase confers processivity on Escherichia coli DNA polymerase I. Proc. Natl. Acad. Sci. U. S. A. 94:1997;479-484.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 479-484
    • Bedford, E.1
  • 51
    • 0023665251 scopus 로고
    • Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7
    • Tabor S., et al. Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7. J. Biol. Chem. 262:1987;16212-16223.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16212-16223
    • Tabor, S.1
  • 52
    • 0035933191 scopus 로고    scopus 로고
    • A type IB topoisomerase with DNA repair activities
    • Belova G.I., et al. A type IB topoisomerase with DNA repair activities. Proc. Natl. Acad. Sci. U. S. A. 98:2001;6015-6020.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 6015-6020
    • Belova, G.I.1
  • 53
    • 0037007150 scopus 로고    scopus 로고
    • The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens
    • Slesarev A.I., et al. The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens. Proc. Natl. Acad. Sci. U. S. A. 99:2002;4644-4649.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 4644-4649
    • Slesarev, A.I.1
  • 54
    • 2342473797 scopus 로고    scopus 로고
    • Use of fimers to eliminate polymerase chain reaction and primer-dimer artifacts and to increase yield in BAC-sequencing reactions
    • S. Zhao, & M. Stodolsky. Humana Press
    • Malykh A.G., et al. Use of fimers to eliminate polymerase chain reaction and primer-dimer artifacts and to increase yield in BAC-sequencing reactions. Zhao S., Stodolsky M. Bacterial Artificial Chromosomes. 2004;221-229 Humana Press.
    • (2004) Bacterial Artificial Chromosomes , pp. 221-229
    • Malykh, A.G.1
  • 55
    • 0024335104 scopus 로고
    • Highly efficient DNA synthesis by the phage φ29 DNA polymerase. Symmetrical mode of DNA replication
    • Blanco L., et al. Highly efficient DNA synthesis by the phage φ29 DNA polymerase. Symmetrical mode of DNA replication. J. Biol. Chem. 264:1989;8935-8940.
    • (1989) J. Biol. Chem. , vol.264 , pp. 8935-8940
    • Blanco, L.1
  • 56
    • 0035890599 scopus 로고    scopus 로고
    • Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): An archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol η
    • Boudsocq F., et al. Sulfolobus solfataricus P2 DNA polymerase IV (Dpo4): an archaeal DinB-like DNA polymerase with lesion-bypass properties akin to eukaryotic pol η Nucleic Acids Res. 29:2001;4607-4616.
    • (2001) Nucleic Acids Res. , vol.29 , pp. 4607-4616
    • Boudsocq, F.1
  • 57
    • 0037053286 scopus 로고    scopus 로고
    • Analysis of a multicomponent thermostable DNA polymerase III replicase from an extreme thermophile
    • Bruck I., et al. Analysis of a multicomponent thermostable DNA polymerase III replicase from an extreme thermophile. J. Biol. Chem. 277:2002;17334-17348.
    • (2002) J. Biol. Chem. , vol.277 , pp. 17334-17348
    • Bruck, I.1
  • 58
    • 0037134533 scopus 로고    scopus 로고
    • DNA polymerase III holoenzyme from Thermus thermophilus identification, expression, purification of components, and use to reconstitute a processive replicase
    • Bullard J.M., et al. DNA polymerase III holoenzyme from Thermus thermophilus identification, expression, purification of components, and use to reconstitute a processive replicase. J. Biol. Chem. 277:2002;13401-13408.
    • (2002) J. Biol. Chem. , vol.277 , pp. 13401-13408
    • Bullard, J.M.1
  • 59
    • 0030666190 scopus 로고    scopus 로고
    • Characterization of DNA polymerase from Pyrococcus sp. strain KOD1 and its application to PCR
    • Takagi M., et al. Characterization of DNA polymerase from Pyrococcus sp. strain KOD1 and its application to PCR. Appl. Environ. Microbiol. 63:1997;4504-4510.
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 4504-4510
    • Takagi, M.1
  • 60
    • 0027494112 scopus 로고
    • High-level expression, purification, and enzymatic characterization of full-length Thermus aquaticus DNA polymerase and a truncated form deficient in 5′ to 3′ exonuclease activity
    • Lawyer F.C., et al. High-level expression, purification, and enzymatic characterization of full-length Thermus aquaticus DNA polymerase and a truncated form deficient in 5′ to 3′ exonuclease activity. PCR Methods Appl. 2:1993;275-287.
    • (1993) PCR Methods Appl. , vol.2 , pp. 275-287
    • Lawyer, F.C.1
  • 61
    • 0027494112 scopus 로고
    • High-level expression, purification, and enzymatic characterization of full-length Thermys aquaticus DNA polymerase and a truncated form deficient in 5′ to 3′ exonuclease activity
    • Lawyer F.C., et al. High-level expression, purification, and enzymatic characterization of full-length Thermys aquaticus DNA polymerase and a truncated form deficient in 5′ to 3′ exonuclease activity. PCR Methods Appl. 2:1993;275-287.
    • (1993) PCR Methods Appl , vol.2 , pp. 275-287
    • Lawyer, F.C.1
  • 62
    • 0027391640 scopus 로고
    • Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities
    • Kong H., et al. Characterization of a DNA polymerase from the hyperthermophile archaea Thermococcus litoralis. Vent DNA polymerase, steady state kinetics, thermal stability, processivity, strand displacement, and exonuclease activities. J. Biol. Chem. 268:1993;1965-1975.
    • (1993) J. Biol. Chem. , vol.268 , pp. 1965-1975
    • Kong, H.1
  • 63
    • 0025315366 scopus 로고
    • High fidelity DNA synthesis by the Thermus aquaticus DNA polymerase
    • Eckert K.A., Kunkel T.A. High fidelity DNA synthesis by the Thermus aquaticus DNA polymerase. Nucleic Acids Res. 18:1990;3739-3744.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 3739-3744
    • Eckert, K.A.1    Kunkel, T.A.2
  • 64
    • 0025739370 scopus 로고
    • Fidelity of Thermococcus litoralis DNA polymerase (Vent™) in PCR determined by denaturing gel electrophoresis
    • Cariello N.F., et al. Fidelity of Thermococcus litoralis DNA polymerase (Vent™) in PCR determined by denaturing gel electrophoresis. Nucleic Acids Res. 19:1991;4193-4198.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4193-4198
    • Cariello, N.F.1
  • 66
    • 0029838624 scopus 로고    scopus 로고
    • PCR fidelity of Pfu DNA polymerase and other thermostable DNA polymerases
    • Cline J., et al. PCR fidelity of Pfu DNA polymerase and other thermostable DNA polymerases. Nucleic Acids Res. 24:1996;3546-3551.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 3546-3551
    • Cline, J.1
  • 67
    • 0032144049 scopus 로고    scopus 로고
    • Pressure enhances thermal stability of DNA polymerase from three thermophilic organisms
    • Summit M., et al. Pressure enhances thermal stability of DNA polymerase from three thermophilic organisms. Extremophiles. 2:1998;339-345.
    • (1998) Extremophiles , vol.2 , pp. 339-345
    • Summit, M.1
  • 68
    • 0025788241 scopus 로고
    • High-fidelity amplification using a thermostable DNA polymerase from Pyrococcus furiosus
    • Lundberg K.S., et al. High-fidelity amplification using a thermostable DNA polymerase from Pyrococcus furiosus. Gene. 108:1991;1-6.
    • (1991) Gene , vol.108 , pp. 1-6
    • Lundberg, K.S.1
  • 69
    • 0027331489 scopus 로고
    • Improved polymerase fidelity in PCR-SSCPA
    • Brail L., et al. Improved polymerase fidelity in PCR-SSCPA. Mutat. Res. 303:1993;171-175.
    • (1993) Mutat. Res. , vol.303 , pp. 171-175
    • Brail, L.1
  • 70
    • 0029793878 scopus 로고    scopus 로고
    • Fidelity and predominant mutations produced by deep vent wild-type and exonuclease-deficient DNA polymerases during in vitro DNA amplification
    • Huang H., Keohavong P. Fidelity and predominant mutations produced by deep vent wild-type and exonuclease-deficient DNA polymerases during in vitro DNA amplification. DNA Cell Biol. 15:1996;589-594.
    • (1996) DNA Cell Biol. , vol.15 , pp. 589-594
    • Huang, H.1    Keohavong, P.2
  • 71
    • 0027198879 scopus 로고
    • Mutational analysis using denaturing gradient gel electrophoresis and PCR
    • Cariello N.F., Skopek T.R. Mutational analysis using denaturing gradient gel electrophoresis and PCR. Mutat. Res. 288:1993;103-112.
    • (1993) Mutat. Res. , vol.288 , pp. 103-112
    • Cariello, N.F.1    Skopek, T.R.2
  • 72
    • 0004062151 scopus 로고
    • Demonstration of the Expand™ PCR system's greater fidelity and higher yields with a lacI-based PCR fidelity assay
    • Frey B., Suppmann B. Demonstration of the Expand™ PCR system's greater fidelity and higher yields with a lacI-based PCR fidelity assay. Biochemica. 2:1995;8-9.
    • (1995) Biochemica , vol.2 , pp. 8-9
    • Frey, B.1    Suppmann, B.2
  • 73
    • 0026637033 scopus 로고
    • Purification and characterization of DNA polymerases from Bacillus species
    • Sellmann E., et al. Purification and characterization of DNA polymerases from Bacillus species. J. Bacteriol. 174:1992;4350-4355.
    • (1992) J. Bacteriol. , vol.174 , pp. 4350-4355
    • Sellmann, E.1
  • 74
    • 0025483642 scopus 로고
    • Purification of a thermostable DNA polymerase from Thermus thermophilus HB8, useful in the polymerase chain reaction
    • Carballeira N., et al. Purification of a thermostable DNA polymerase from Thermus thermophilus HB8, useful in the polymerase chain reaction. Biotechniques. 9:1990;276-281.
    • (1990) Biotechniques , vol.9 , pp. 276-281
    • Carballeira, N.1
  • 75
    • 0025764762 scopus 로고
    • Fidelity of DNA synthesis by the Thermococcus litoralis DNA polymerase - An extremely heat stable enzyme with proofreading activity
    • Mattila P., et al. Fidelity of DNA synthesis by the Thermococcus litoralis DNA polymerase - an extremely heat stable enzyme with proofreading activity. Nucleic Acids Res. 19:1991;4967-4973.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4967-4973
    • Mattila, P.1
  • 76
    • 17044446557 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of DNA polymerase I from the hyperthermophilic archaea Thermococcus fumicolans
    • Cambon-Bonavita M.-A., et al. Cloning, expression, and characterization of DNA polymerase I from the hyperthermophilic archaea Thermococcus fumicolans. Extremophiles. 4:2000;215-225.
    • (2000) Extremophiles , vol.4 , pp. 215-225
    • Cambon-Bonavita, M.-A.1
  • 77
    • 0034667769 scopus 로고    scopus 로고
    • PCR performance of the B-type DNA polymerase from the thermophilic euryarchaeon Thermococcus aggregans improved by mutations in the Y-GG/A motif
    • Bohlke K., et al. PCR performance of the B-type DNA polymerase from the thermophilic euryarchaeon Thermococcus aggregans improved by mutations in the Y-GG/A motif. Nucleic Acids Res. 28:2000;3910-3917.
    • (2000) Nucleic Acids Res. , vol.28 , pp. 3910-3917
    • Bohlke, K.1
  • 79
    • 0030921648 scopus 로고    scopus 로고
    • Fidelity and mutational spectrum of Pfu DNA polymerase on a human mitochondrial DNA sequence
    • Andre P., et al. Fidelity and mutational spectrum of Pfu DNA polymerase on a human mitochondrial DNA sequence. Genome Res. 7:1997;843-852.
    • (1997) Genome Res. , vol.7 , pp. 843-852
    • Andre, P.1
  • 80
    • 0037137278 scopus 로고    scopus 로고
    • PCR performance of the highly thermostable proof-reading B-type DNA polymerase from Pyrococcus abyssi
    • Dietrich J., et al. PCR performance of the highly thermostable proof-reading B-type DNA polymerase from Pyrococcus abyssi. FEMS Microbiol. Lett. 217:2002;89-94.
    • (2002) FEMS Microbiol. Lett. , vol.217 , pp. 89-94
    • Dietrich, J.1
  • 81
    • 0040877043 scopus 로고    scopus 로고
    • Cloning and characterization of a family B DNA polymerase form the hyperthermophilic chrenarchaeon Pyrobaculum islandicum
    • Kahler M., Antranikian G. Cloning and characterization of a family B DNA polymerase form the hyperthermophilic chrenarchaeon Pyrobaculum islandicum. J. Bacteriol. 182:2000;655-663.
    • (2000) J. Bacteriol. , vol.182 , pp. 655-663
    • Kahler, M.1    Antranikian, G.2
  • 82
    • 0037205402 scopus 로고    scopus 로고
    • Low fidelity DNA synthesis by a Y-family DNA polymerase due to misalignment in the active site
    • Kokoska R.J., et al. Low fidelity DNA synthesis by a Y-family DNA polymerase due to misalignment in the active site. J. Biol. Chem. 277:2002;19633-19638.
    • (2002) J. Biol. Chem. , vol.277 , pp. 19633-19638
    • Kokoska, R.J.1
  • 83
    • 0034864429 scopus 로고    scopus 로고
    • Cloning, sequence analysis and functional characterization of DNA polymerase I from the thermophilic eubacterium Rhodothermus marinus
    • Blondal T., et al. Cloning, sequence analysis and functional characterization of DNA polymerase I from the thermophilic eubacterium Rhodothermus marinus. Biotechnol. Appl. Biochem. 34:2001;37-45.
    • (2001) Biotechnol. Appl. Biochem. , vol.34 , pp. 37-45
    • Blondal, T.1
  • 84
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis D.L., et al. Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP. Nature. 313:1985;762-766.
    • (1985) Nature , vol.313 , pp. 762-766
    • Ollis, D.L.1
  • 85
    • 0023242425 scopus 로고
    • An improved method for prenatal diagnosis of genetic diseases by analysis of amplified DNA sequences. Application to hemophilia A
    • Kogan S.C., et al. An improved method for prenatal diagnosis of genetic diseases by analysis of amplified DNA sequences. application to hemophilia A. N. Engl. J. Med. 317:1987;985-990.
    • (1987) N. Engl. J. Med. , vol.317 , pp. 985-990
    • Kogan, S.C.1
  • 86
    • 0028211009 scopus 로고
    • PCR amplification of up to 35-kb DNA with high fidelity and high yield from λ bacteriophage templates
    • Barnes W. PCR amplification of up to 35-kb DNA with high fidelity and high yield from λ bacteriophage templates. Proc. Natl. Acad. Sci. U. S. A. 91:1994;2216-2220.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 2216-2220
    • Barnes, W.1
  • 87
    • 0027163526 scopus 로고
    • Crystal structure of bacteriophage T7 RNA polymerase at 3.3 a resolution
    • Sousa R., et al. Crystal structure of bacteriophage T7 RNA polymerase at 3.3 A resolution. Nature. 364:1993;593-599.
    • (1993) Nature , vol.364 , pp. 593-599
    • Sousa, R.1
  • 88
    • 0031587827 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69
    • Wang J., et al. Crystal structure of a pol alpha family replication DNA polymerase from bacteriophage RB69. Cell. 89:1997;1087-1099.
    • (1997) Cell , vol.89 , pp. 1087-1099
    • Wang, J.1
  • 89
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution
    • Doublie S., et al. Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution. Nature. 391:1998;251-258.
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublie, S.1
  • 90
    • 1942459076 scopus 로고    scopus 로고
    • Thermophilic polymerases from Thermotoga neapolitanana US Patent 6,001,645.
    • Slater, M. R et al. (1999) Thermophilic polymerases from Thermotoga neapolitanana US Patent 6,001,645.
    • (1999)
    • Slater, M.R.1
  • 91
    • 1942427194 scopus 로고    scopus 로고
    • Method for cloning and expression of Rhodothermus obamensis DNA polymerase I large fragment in E. coli. US Patent 6,440,715.
    • Xu, S. (2002) Method for cloning and expression of Rhodothermus obamensis DNA polymerase I large fragment in E. coli. US Patent 6,440,715.
    • (2002)
    • Xu, S.1
  • 92
    • 1942523391 scopus 로고    scopus 로고
    • Purified Thermococcus barossi DNA polymerase US Patent 5,602,011.
    • Luhm, R.A. et al. (1997) Purified Thermococcus barossi DNA polymerase US Patent 5,602,011.
    • (1997)
    • Luhm, R.A.1
  • 93
    • 1942459077 scopus 로고    scopus 로고
    • Method for cloning and producing Thermomicrobium roseum DNA US Patent 5, 962,296.
    • Etwiller, L. and Xu, Shuang-yong (1999) Method for cloning and producing Thermomicrobium roseum DNA US Patent 5, 962,296.
    • (1999)
    • Etwiller, L.1    Xu, S.-Y.2
  • 94
    • 1942523392 scopus 로고    scopus 로고
    • Thermostable DNA polymerase from Carboxythermus hydrogenoformans US Patent 6,468,775.
    • Ankenbauer, W. et al. (2002) Thermostable DNA polymerase from Carboxythermus hydrogenoformans US Patent 6,468,775.
    • (2002)
    • Ankenbauer, W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.