메뉴 건너뛰기




Volumn 18, Issue 4, 2014, Pages 653-664

Characterization of Family D DNA polymerase from Thermococcus sp. 9°N

Author keywords

Analytical biochemistry; Archaea; DNA enzymes; DNA polymerase; DNA replication; Family D DNA polymerase; Fidelity; Replisome; Thermococcus

Indexed keywords

ARCHAEA; CRENARCHAEOTA; ESCHERICHIA COLI; METHANOCOCCUS MARIPALUDIS; THERMOCOCCUS; THERMOCOCCUS KODAKARENSIS; THERMOCOCCUS SP.;

EID: 84903200167     PISSN: 14310651     EISSN: 14334909     Source Type: Journal    
DOI: 10.1007/s00792-014-0646-9     Document Type: Article
Times cited : (22)

References (53)
  • 1
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism
    • Beese LS, Steitz TA (1991) Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: a two metal ion mechanism. EMBO J 10(1): 25-33.
    • (1991) EMBO J , vol.10 , Issue.1 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 2
    • 34447319079 scopus 로고    scopus 로고
    • Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1
    • Berquist BR, DasSarma P, DasSarma S (2007) Essential and non-essential DNA replication genes in the model halophilic Archaeon, Halobacterium sp. NRC-1. BMC Genet 8: 31.
    • (2007) BMC Genet , vol.8 , pp. 31
    • Berquist, B.R.1    DasSarma, P.2    DasSarma, S.3
  • 3
    • 0027217643 scopus 로고
    • Compilation, alignment, and phylogenetic relationships of DNA polymerases
    • Braithwaite DK, Ito J (1993) Compilation, alignment, and phylogenetic relationships of DNA polymerases. Nucleic Acids Res 21(4): 787-802.
    • (1993) Nucleic Acids Res , vol.21 , Issue.4 , pp. 787-802
    • Braithwaite, D.K.1    Ito, J.2
  • 4
    • 0032564361 scopus 로고    scopus 로고
    • A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase
    • Cann IK, Komori K, Toh H, Kanai S, Ishino Y (1998) A heterodimeric DNA polymerase: evidence that members of Euryarchaeota possess a distinct DNA polymerase. Proc Natl Acad Sci USA 95(24): 14250-14255.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.24 , pp. 14250-14255
    • Cann, I.K.1    Komori, K.2    Toh, H.3    Kanai, S.4    Ishino, Y.5
  • 6
    • 0026085471 scopus 로고
    • 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 ND, Joyce CM (1991) The 3′-5′ exonuclease of DNA polymerase I of Escherichia coli: contribution of each amino acid at the active site to the reaction. EMBO J 10(1): 17-24.
    • (1991) EMBO J , vol.10 , Issue.1 , pp. 17-24
    • Derbyshire, V.1    Grindley, N.D.2    Joyce, C.M.3
  • 7
    • 0027448958 scopus 로고
    • Mutational studies of human DNA polymerase alpha. Identification of residues critical for deoxynucleotide binding and misinsertion fidelity of DNA synthesis
    • Dong Q, Copeland WC, Wang TS (1993) Mutational studies of human DNA polymerase alpha. Identification of residues critical for deoxynucleotide binding and misinsertion fidelity of DNA synthesis. J Biol Chem 268(32): 24163-24174.
    • (1993) J Biol Chem , vol.268 , Issue.32 , pp. 24163-24174
    • Dong, Q.1    Copeland, W.C.2    Wang, T.S.3
  • 8
    • 0032543992 scopus 로고    scopus 로고
    • Unequal fidelity of leading strand and lagging strand DNA replication on the Escherichia coli chromosome
    • Fijalkowska IJ, Jonczyk P, Tkaczyk MM, Bialoskorska M, Schaaper RM (1998) Unequal fidelity of leading strand and lagging strand DNA replication on the Escherichia coli chromosome. Proc Natl Acad Sci USA 95(17): 10020-10025.
    • (1998) Proc Natl Acad Sci USA , vol.95 , Issue.17 , pp. 10020-10025
    • Fijalkowska, I.J.1    Jonczyk, P.2    Tkaczyk, M.M.3    Bialoskorska, M.4    Schaaper, R.M.5
  • 9
    • 79957471219 scopus 로고    scopus 로고
    • Enzymatic assembly of overlapping DNA fragments
    • Gibson DG (2011) Enzymatic assembly of overlapping DNA fragments. Methods Enzymol 498: 349-361.
    • (2011) Methods Enzymol , vol.498 , pp. 349-361
    • Gibson, D.G.1
  • 11
    • 84866865361 scopus 로고    scopus 로고
    • In vitro reconstitution of RNA primer removal in Archaea reveals the existence of two pathways
    • Henneke G (2012) In vitro reconstitution of RNA primer removal in Archaea reveals the existence of two pathways. Biochem J 447(2): 271-280.
    • (2012) Biochem J , vol.447 , Issue.2 , pp. 271-280
    • Henneke, G.1
  • 12
    • 20444377771 scopus 로고    scopus 로고
    • The hyperthermophilic euryarchaeota Pyrococcus abyssi likely requires the two DNA polymerases D and B for DNA replication
    • Henneke G, Flament D, Hübscher U, Querellou J, Raffin J-P (2005) The hyperthermophilic euryarchaeota Pyrococcus abyssi likely requires the two DNA polymerases D and B for DNA replication. J Mol Biol 350(1): 53-64.
    • (2005) J Mol Biol , vol.350 , Issue.1 , pp. 53-64
    • Henneke, G.1    Flament, D.2    Hübscher, U.3    Querellou, J.4    Raffin, J.-P.5
  • 13
    • 33749033347 scopus 로고    scopus 로고
    • The replication clamp-loading machine at work in the three domains of life
    • Indiani C, O'Donnell M (2006) The replication clamp-loading machine at work in the three domains of life. Nat Rev Mol Cell Biol 7(10): 751-761.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.10 , pp. 751-761
    • Indiani, C.1    O'Donnell, M.2
  • 14
    • 84861692094 scopus 로고    scopus 로고
    • Rapid progress of DNA replication studies in Archaea, the third domain of life
    • doi:10.1007/s11427-012-4324-9
    • Ishino Y, Ishino S (2012) Rapid progress of DNA replication studies in Archaea, the third domain of life. Science China Life Sci 55(5): 386-403. doi: 10. 1007/s11427-012-4324-9.
    • (2012) Science China Life Sci , vol.55 , Issue.5 , pp. 386-403
    • Ishino, Y.1    Ishino, S.2
  • 15
    • 0031922356 scopus 로고    scopus 로고
    • A novel DNA polymerase family found in Archaea
    • Ishino Y, Komori K, Cann IK, Koga Y (1998) A novel DNA polymerase family found in Archaea. J Bacteriol 180(8): 2232-2236.
    • (1998) J Bacteriol , vol.180 , Issue.8 , pp. 2232-2236
    • Ishino, Y.1    Komori, K.2    Cann, I.K.3    Koga, Y.4
  • 16
    • 2342597828 scopus 로고    scopus 로고
    • Characterization of the 3′-5′ exonuclease subunit DP1 of Methanococcus jannaschii replicative DNA polymerase D
    • Jokela M, Eskelinen A, Pospiech H, Rouvinen J, Syväoja JE (2004) Characterization of the 3′-5′ exonuclease subunit DP1 of Methanococcus jannaschii replicative DNA polymerase D. Nucleic Acids Res 32(8): 2430-2440.
    • (2004) Nucleic Acids Res , vol.32 , Issue.8 , pp. 2430-2440
    • Jokela, M.1    Eskelinen, A.2    Pospiech, H.3    Rouvinen, J.4    Syväoja, J.E.5
  • 17
    • 23244462784 scopus 로고    scopus 로고
    • The screening of expression and purification conditions for replicative DNA polymerase associated B-subunits, assignment of the exonuclease activity to the C-terminus of archaeal pol D DP1 subunit
    • Jokela M, Raki M, Heikkinen K, Sepponen K, Eskelinen A, Syväoja JE (2005) The screening of expression and purification conditions for replicative DNA polymerase associated B-subunits, assignment of the exonuclease activity to the C-terminus of archaeal pol D DP1 subunit. Protein Express Purif 43(1): 73-84.
    • (2005) Protein Express Purif , vol.43 , Issue.1 , pp. 73-84
    • Jokela, M.1    Raki, M.2    Heikkinen, K.3    Sepponen, K.4    Eskelinen, A.5    Syväoja, J.E.6
  • 18
    • 0028881713 scopus 로고
    • Polymerase structures and function: variations on a theme?
    • Joyce CM, Steitz TA (1995) Polymerase structures and function: variations on a theme? J Bacteriol 177(22): 6321-6329.
    • (1995) J Bacteriol , vol.177 , Issue.22 , pp. 6321-6329
    • Joyce, C.M.1    Steitz, T.A.2
  • 19
    • 0344011118 scopus 로고    scopus 로고
    • Cold-sensitive mutants of Taq DNA polymerase provide a hot start for PCR
    • Kermekchiev MB, Tzekov A, Barnes WM (2003) Cold-sensitive mutants of Taq DNA polymerase provide a hot start for PCR. Nucleic Acids Res 31(21): 6139-6147.
    • (2003) Nucleic Acids Res , vol.31 , Issue.21 , pp. 6139-6147
    • Kermekchiev, M.B.1    Tzekov, A.2    Barnes, W.M.3
  • 20
    • 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, Kucera RB, Jack WE (1993) 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(3): 1965-1975.
    • (1993) J Biol Chem , vol.268 , Issue.3 , pp. 1965-1975
    • Kong, H.1    Kucera, R.B.2    Jack, W.E.3
  • 21
    • 0019810626 scopus 로고
    • Aphidicolin inhibits DNA synthesis by DNA polymerase alpha and isolated nuclei by a similar mechanism
    • Krokan H, Wist E, Krokan RH (1981) Aphidicolin inhibits DNA synthesis by DNA polymerase alpha and isolated nuclei by a similar mechanism. Nucleic Acids Res 9(18): 4709-4719.
    • (1981) Nucleic Acids Res , vol.9 , Issue.18 , pp. 4709-4719
    • Krokan, H.1    Wist, E.2    Krokan, R.H.3
  • 22
    • 84868097664 scopus 로고    scopus 로고
    • Comparative analyses of the two proliferating cell nuclear antigens from the hyperthermophilic archaeon, Thermococcus kodakarensis
    • Kuba Y, Ishino S, Yamagami T, Tokuhara M, Kanai T, Fujikane R, Daiyasu H, Atomi H, Ishino Y (2012) Comparative analyses of the two proliferating cell nuclear antigens from the hyperthermophilic archaeon, Thermococcus kodakarensis. Genes Cells 17(11): 923-937.
    • (2012) Genes Cells , vol.17 , Issue.11 , pp. 923-937
    • Kuba, Y.1    Ishino, S.2    Yamagami, T.3    Tokuhara, M.4    Kanai, T.5    Fujikane, R.6    Daiyasu, H.7    Atomi, H.8    Ishino, Y.9
  • 23
    • 77957740230 scopus 로고    scopus 로고
    • Evolving views of DNA replication (in)fidelity
    • Kunkel TA (2009) Evolving views of DNA replication (in)fidelity. Cold Spring Harbor Symp Quant Biol 74: 91-101.
    • (2009) Cold Spring Harbor Symp Quant Biol , vol.74 , pp. 91-101
    • Kunkel, T.A.1
  • 24
    • 79952610080 scopus 로고    scopus 로고
    • Crystal structures of two active proliferating cell nuclear antigens (PCNAs) encoded by Thermococcus kodakaraensis
    • Ladner JE, Pan M, Hurwitz J, Kelman Z (2011) Crystal structures of two active proliferating cell nuclear antigens (PCNAs) encoded by Thermococcus kodakaraensis. Proc Natl Acad Sci USA 108(7): 2711-2716.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.7 , pp. 2711-2716
    • Ladner, J.E.1    Pan, M.2    Hurwitz, J.3    Kelman, Z.4
  • 25
    • 79952125243 scopus 로고    scopus 로고
    • Affinity purification of an archaeal DNA replication protein network
    • Li Z, Santangelo TJ, Cuboňová L, Reeve JN, Kelman Z (2010) Affinity purification of an archaeal DNA replication protein network. mBio 1 (5).
    • (2010) MBio , vol.1 , Issue.5
    • Li, Z.1    Santangelo, T.J.2    Cuboňová, L.3    Reeve, J.N.4    Kelman, Z.5
  • 27
    • 84873151038 scopus 로고    scopus 로고
    • Thermococcus kodakarensis DNA replication
    • Li Z, Kelman LM, Kelman Z (2013) Thermococcus kodakarensis DNA replication. Biochem Soc Trans 41(1): 332-338.
    • (2013) Biochem Soc Trans , vol.41 , Issue.1 , pp. 332-338
    • Li, Z.1    Kelman, L.M.2    Kelman, Z.3
  • 28
    • 79551469840 scopus 로고    scopus 로고
    • Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii
    • Matsui I, Urushibata Y, Shen Y, Matsui E, Yokoyama H (2011) Novel structure of an N-terminal domain that is crucial for the dimeric assembly and DNA-binding of an archaeal DNA polymerase D large subunit from Pyrococcus horikoshii. FEBS Lett 585(3): 452-458.
    • (2011) FEBS Lett , vol.585 , Issue.3 , pp. 452-458
    • Matsui, I.1    Urushibata, Y.2    Shen, Y.3    Matsui, E.4    Yokoyama, H.5
  • 29
    • 0025764762 scopus 로고
    • Fidelity of DNA synthesis by the Thermococcus litoralis DNA polymerase-an extremely heat stable enzyme with proofreading activity
    • Mattila P, Korpela J, Tenkanen T, Pitkänen K (1991) Fidelity of DNA synthesis by the Thermococcus litoralis DNA polymerase-an extremely heat stable enzyme with proofreading activity. Nucleic Acids Res 19(18): 4967-4973.
    • (1991) Nucleic Acids Res , vol.19 , Issue.18 , pp. 4967-4973
    • Mattila, P.1    Korpela, J.2    Tenkanen, T.3    Pitkänen, K.4
  • 31
    • 80053560927 scopus 로고    scopus 로고
    • Bacterial replicases and related polymerases
    • McHenry CS (2011) Bacterial replicases and related polymerases. Curr Opin Chem Biol 15(5): 587-594.
    • (2011) Curr Opin Chem Biol , vol.15 , Issue.5 , pp. 587-594
    • McHenry, C.S.1
  • 35
    • 0036084146 scopus 로고    scopus 로고
    • InBase: the Intein Database
    • Perler FB (2002) InBase: the Intein Database. Nucleic Acids Res 30(1): 383-384.
    • (2002) Nucleic Acids Res , vol.30 , Issue.1 , pp. 383-384
    • Perler, F.B.1
  • 37
    • 0032483332 scopus 로고    scopus 로고
    • The base substitution and frameshift fidelity of Escherichia coli DNA polymerase III holoenzyme in vitro
    • Pham PT, Olson MW, McHenry CS, Schaaper RM (1998) The base substitution and frameshift fidelity of Escherichia coli DNA polymerase III holoenzyme in vitro. J Biol Chem 273(36): 23575-23584.
    • (1998) J Biol Chem , vol.273 , Issue.36 , pp. 23575-23584
    • Pham, P.T.1    Olson, M.W.2    McHenry, C.S.3    Schaaper, R.M.4
  • 38
    • 77949568225 scopus 로고    scopus 로고
    • DNA polymerase proofreading: multiple roles maintain genome stability
    • Reha-Krantz LJ (2010) DNA polymerase proofreading: multiple roles maintain genome stability. Biochim Biophys Acta 1804(5): 1049-1063.
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.5 , pp. 1049-1063
    • Reha-Krantz, L.J.1
  • 39
    • 0034595517 scopus 로고    scopus 로고
    • Crystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7
    • Rodriguez A, Park H, Mao C, Beese L (2000) Crystal structure of a pol alpha family DNA polymerase from the hyperthermophilic archaeon Thermococcus sp. 9 degrees N-7. J Mol Biol 299(2): 447-462.
    • (2000) J Mol Biol , vol.299 , Issue.2 , pp. 447-462
    • Rodriguez, A.1    Park, H.2    Mao, C.3    Beese, L.4
  • 40
    • 34247628927 scopus 로고    scopus 로고
    • DNA polymerase switching on homotrimeric PCNA at the replication fork of the euryarchaeota Pyrococcus abyssi
    • Rouillon C, Henneke G, Flament D, Querellou J, Raffin J-P (2007) DNA polymerase switching on homotrimeric PCNA at the replication fork of the euryarchaeota Pyrococcus abyssi. J Mol Biol 369(2): 343-355.
    • (2007) J Mol Biol , vol.369 , Issue.2 , pp. 343-355
    • Rouillon, C.1    Henneke, G.2    Flament, D.3    Querellou, J.4    Raffin, J.-P.5
  • 41
    • 84875251958 scopus 로고    scopus 로고
    • Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis
    • Sarmiento F, Mrazek J, Whitman WB (2013) Genome-scale analysis of gene function in the hydrogenotrophic methanogenic archaeon Methanococcus maripaludis. Proc Natl Acad Sci USA 110(12): 4726-4731.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.12 , pp. 4726-4731
    • Sarmiento, F.1    Mrazek, J.2    Whitman, W.B.3
  • 43
    • 0035920137 scopus 로고    scopus 로고
    • Invariant Asp-1122 and Asp-1124 are essential residues for polymerization catalysis of family D DNA polymerase from Pyrococcus horikoshii
    • Shen Y, Musti K, Hiramoto M, Kikuchi H, Kawarabayashi Y, Matsui I (2001) Invariant Asp-1122 and Asp-1124 are essential residues for polymerization catalysis of family D DNA polymerase from Pyrococcus horikoshii. J Biol Chem 276(29): 27376-27383.
    • (2001) J Biol Chem , vol.276 , Issue.29 , pp. 27376-27383
    • Shen, Y.1    Musti, K.2    Hiramoto, M.3    Kikuchi, H.4    Kawarabayashi, Y.5    Matsui, I.6
  • 44
    • 0038079801 scopus 로고    scopus 로고
    • Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii
    • Shen Y, Tang X-F, Matsui I (2003) Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii. J Biol Chem 278(23): 21247-21257.
    • (2003) J Biol Chem , vol.278 , Issue.23 , pp. 21247-21257
    • Shen, Y.1    Tang, X.-F.2    Matsui, I.3
  • 45
    • 2342586707 scopus 로고    scopus 로고
    • Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii
    • Shen Y, Tang X-F, Matsui E, Matsui I (2004a) Subunit interaction and regulation of activity through terminal domains of the family D DNA polymerase from Pyrococcus horikoshii. Biochem Soc Trans 32(Pt 2): 245-249.
    • (2004) Biochem Soc Trans , vol.32 , Issue.Pt 2 , pp. 245-249
    • Shen, Y.1    Tang, X.-F.2    Matsui, E.3    Matsui, I.4
  • 46
    • 1242331846 scopus 로고    scopus 로고
    • A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulates its nuclease activity which is Mre11-like and prefers manganese ion as the cofactor
    • Shen Y, Tang X-F, Yokoyama H, Matsui E, Matsui I (2004b) A 21-amino acid peptide from the cysteine cluster II of the family D DNA polymerase from Pyrococcus horikoshii stimulates its nuclease activity which is Mre11-like and prefers manganese ion as the cofactor. Nucleic Acids Res 32(1): 158-168.
    • (2004) Nucleic Acids Res , vol.32 , Issue.1 , pp. 158-168
    • Shen, Y.1    Tang, X.-F.2    Yokoyama, H.3    Matsui, E.4    Matsui, I.5
  • 47
    • 0030014622 scopus 로고    scopus 로고
    • Cloning of thermostable DNA polymerases from hyperthermophilic marine Archaea with emphasis on Thermococcus sp. 9 degrees N-7 and mutations affecting 3′-5′ exonuclease activity
    • Southworth MW, Kong H, Kucera RB, Ware J, Jannasch HW, Perler FB (1996) Cloning of thermostable DNA polymerases from hyperthermophilic marine Archaea with emphasis on Thermococcus sp. 9 degrees N-7 and mutations affecting 3′-5′ exonuclease activity. Proc Natl Acad Sci USA 93(11): 5281-5285.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.11 , pp. 5281-5285
    • Southworth, M.W.1    Kong, H.2    Kucera, R.B.3    Ware, J.4    Jannasch, H.W.5    Perler, F.B.6
  • 48
    • 0030897085 scopus 로고    scopus 로고
    • Low fidelity mutants in the O-helix of Thermus aquaticus DNA polymerase I
    • Suzuki M, Avicola AK, Hood L, Loeb LA (1997) Low fidelity mutants in the O-helix of Thermus aquaticus DNA polymerase I. J Biol Chem 272(17): 11228-11235.
    • (1997) J Biol Chem , vol.272 , Issue.17 , pp. 11228-11235
    • Suzuki, M.1    Avicola, A.K.2    Hood, L.3    Loeb, L.A.4
  • 49
    • 4644250659 scopus 로고    scopus 로고
    • Domain topology of the DNA polymerase D complex from a hyperthermophilic archaeon Pyrococcus horikoshii
    • Tang X-F, Shen Y, Matsui E, Matsui I (2004) Domain topology of the DNA polymerase D complex from a hyperthermophilic archaeon Pyrococcus horikoshii. Biochemistry 43(37): 11818-11827.
    • (2004) Biochemistry , vol.43 , Issue.37 , pp. 11818-11827
    • Tang, X.-F.1    Shen, Y.2    Matsui, E.3    Matsui, I.4
  • 50
    • 77955268031 scopus 로고    scopus 로고
    • Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases
    • Yamasaki K, Urushibata Y, Yamasaki T, Arisaka F, Matsui I (2010) Solution structure of the N-terminal domain of the archaeal D-family DNA polymerase small subunit reveals evolutionary relationship to eukaryotic B-family polymerases. FEBS Lett 584(15): 3370-3375.
    • (2010) FEBS Lett , vol.584 , Issue.15 , pp. 3370-3375
    • Yamasaki, K.1    Urushibata, Y.2    Yamasaki, T.3    Arisaka, F.4    Matsui, I.5
  • 51
    • 77949571124 scopus 로고    scopus 로고
    • DNA polymerase family X: function, structure, and cellular roles
    • Yamtich J, Sweasy JB (2010) DNA polymerase family X: function, structure, and cellular roles. Biochim Biophys Acta 1804(5): 1136-1150.
    • (2010) Biochim Biophys Acta , vol.1804 , Issue.5 , pp. 1136-1150
    • Yamtich, J.1    Sweasy, J.B.2
  • 52
    • 68249097023 scopus 로고    scopus 로고
    • Polymerization fidelity of a replicative DNA polymerase from the hyperthermophilic archaeon Sulfolobus solfataricus P2
    • Zhang L, Brown JA, Newmister SA, Suo Z (2009) Polymerization fidelity of a replicative DNA polymerase from the hyperthermophilic archaeon Sulfolobus solfataricus P2. Biochemistry 48(31): 7492-7501.
    • (2009) Biochemistry , vol.48 , Issue.31 , pp. 7492-7501
    • Zhang, L.1    Brown, J.A.2    Newmister, S.A.3    Suo, Z.4
  • 53
    • 72449152986 scopus 로고    scopus 로고
    • Accurate DNA synthesis by Sulfolobus solfataricus DNA polymerase B1 at high temperature
    • Zhang L, Lou H, Guo L, Zhan Z, Duan Z, Guo X, Huang L (2010) Accurate DNA synthesis by Sulfolobus solfataricus DNA polymerase B1 at high temperature. Extremophiles 14(1): 107-117.
    • (2010) Extremophiles , vol.14 , Issue.1 , pp. 107-117
    • Zhang, L.1    Lou, H.2    Guo, L.3    Zhan, Z.4    Duan, Z.5    Guo, X.6    Huang, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.