메뉴 건너뛰기




Volumn 5, Issue APR, 2014, Pages

Bacteriophage T7 DNA polymerase-sequenase

Author keywords

Bacteriophage T7; DNA polymerase; DNA sequencing; Marine phages; Sequenase

Indexed keywords

DNA POLYMERASE; SEQUENASE; UNCLASSIFIED DRUG;

EID: 84899692796     PISSN: None     EISSN: 1664302X     Source Type: Journal    
DOI: 10.3389/fmicb.2014.00181     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 77957014812 scopus 로고    scopus 로고
    • Conformational dynamics of bacteriophage T7 DNA polymerase and its processivity factor, Escherichia coli thioredoxin
    • doi: 10.1073/pnas.1010141107
    • Akabayov, B., Akabayov, S. R., Lee, S. J., Tabor, S., Kulczyk, A. W., and Richardson, C. C. (2010). Conformational dynamics of bacteriophage T7 DNA polymerase and its processivity factor, Escherichia coli thioredoxin. Proc. Natl. Acad. Sci. U.S.A. 107, 15033-15038. doi: 10.1073/pnas.1010141107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15033-15038
    • Akabayov, B.1    Akabayov, S.R.2    Lee, S.J.3    Tabor, S.4    Kulczyk, A.W.5    Richardson, C.C.6
  • 2
    • 0033731729 scopus 로고    scopus 로고
    • A unique loop in the DNA-binding crevice of bacteriophage T7 DNA polymerase influences primer utilization
    • doi: 10.1073/pnas.230448397
    • Chowdhury, K., Tabor, S., and Richardson, C. C. (2000). A unique loop in the DNA-binding crevice of bacteriophage T7 DNA polymerase influences primer utilization. Proc. Natl. Acad. Sci. U.S.A. 97, 12469-12474. doi: 10.1073/pnas.230448397
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 12469-12474
    • Chowdhury, K.1    Tabor, S.2    Richardson, C.C.3
  • 3
    • 0028357737 scopus 로고
    • Coordination of leading and lagging strand DNA synthesis at the replication fork of bacteriophage T7
    • doi: 10.1016/0092-8674(94)90243-7
    • Debyser, Z., Tabor, S., and Richardson, C. C. (1994). Coordination of leading and lagging strand DNA synthesis at the replication fork of bacteriophage T7. Cell 77, 157-166. doi: 10.1016/0092-8674(94)90243-7
    • (1994) Cell , vol.77 , pp. 157-166
    • Debyser, Z.1    Tabor, S.2    Richardson, C.C.3
  • 4
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • doi: 10.1038/34593
    • Doublié, S., Tabor, S., Long, A. M., Richardson, C. C., and Ellenberger, T. (1998). Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution. Nature 391, 251-258. doi: 10.1038/34593
    • (1998) Nature , vol.391 , pp. 251-258
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 5
    • 0021112553 scopus 로고
    • Two forms of the DNA polymerase of bacteriophage T7
    • Engler, M. J., Lechner, R. L., and Richardson, C. C. (1983). Two forms of the DNA polymerase of bacteriophage T7. J. Biol. Chem. 258, 11165-11173.
    • (1983) J. Biol. Chem. , vol.258 , pp. 11165-11173
    • Engler, M.J.1    Lechner, R.L.2    Richardson, C.C.3
  • 6
    • 76649145153 scopus 로고    scopus 로고
    • Thioredoxin suppresses microscopic hopping of T7 DNA polymerase on duplex DNA
    • doi: 10.1073/pnas.0912664107
    • Etson, C. M., Hamdan, S. M., Richardson, C. C., and van Oijen, A. M. (2010). Thioredoxin suppresses microscopic hopping of T7 DNA polymerase on duplex DNA. Proc. Natl. Acad. Sci. U.S.A. 107, 1900-1905. doi: 10.1073/pnas.0912664107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 1900-1905
    • Etson, C.M.1    Hamdan, S.M.2    Richardson, C.C.3    van Oijen, A.M.4
  • 7
    • 0019124781 scopus 로고
    • Bacteriophage T7 DNA replication in vitro. Stimulation of DNA synthesis by T7 RNA polymerase
    • Fischer, H., and Hinkle, D. C. (1980). Bacteriophage T7 DNA replication in vitro. Stimulation of DNA synthesis by T7 RNA polymerase. J. Biol. Chem. 255, 7956-7964.
    • (1980) J. Biol. Chem. , vol.255 , pp. 7956-7964
    • Fischer, H.1    Hinkle, D.C.2
  • 8
    • 84896503280 scopus 로고    scopus 로고
    • Single-molecule studies of polymerase dynamics and stoichiometry at the bacteriophage T7 replication machinery
    • doi: 10.1073/pnas.1402010111 [Epub ahead of print].
    • Geertsema, H. J., Kulczyk, A. W., Richardson, C. C., and van Oijen, A. M. (2014). Single-molecule studies of polymerase dynamics and stoichiometry at the bacteriophage T7 replication machinery. Proc. Natl. Acad. Sci. U.S.A. doi: 10.1073/pnas.1402010111 [Epub ahead of print].
    • (2014) Proc. Natl. Acad. Sci. U.S.A.
    • Geertsema, H.J.1    Kulczyk, A.W.2    Richardson, C.C.3    van Oijen, A.M.4
  • 9
    • 57649131058 scopus 로고    scopus 로고
    • Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase
    • doi: 10.1074/jbc.M805062200
    • Ghosh, S., Hamdan, S. M., Cook, T. E., and Richardson, C. C. (2008). Interactions of Escherichia coli thioredoxin, the processivity factor, with bacteriophage T7 DNA polymerase and helicase. J. Biol. Chem. 283, 32077-32084. doi: 10.1074/jbc.M805062200
    • (2008) J. Biol. Chem. , vol.283 , pp. 32077-32084
    • Ghosh, S.1    Hamdan, S.M.2    Cook, T.E.3    Richardson, C.C.4
  • 10
    • 77952917694 scopus 로고    scopus 로고
    • Two modes of interaction of the single-stranded DNA-binding protein of bacteriophage T7 with the DNA polymerase-thioredoxin complex
    • doi: 10.1074/jbc.M110.107656
    • Ghosh, S., Hamdan, S. M., and Richardson, C. C. (2010). Two modes of interaction of the single-stranded DNA-binding protein of bacteriophage T7 with the DNA polymerase-thioredoxin complex. J. Biol. Chem. 285, 18103-18112. doi: 10.1074/jbc.M110.107656
    • (2010) J. Biol. Chem. , vol.285 , pp. 18103-18112
    • Ghosh, S.1    Hamdan, S.M.2    Richardson, C.C.3
  • 11
    • 71049114220 scopus 로고    scopus 로고
    • C-terminal phenylalanine of bacteriophage T7 single-stranded DNA-binding protein is essential for strand displacement synthesis by T7 DNA polymerase at a nick in DNA
    • doi: 10.1074/jbc.M109.024059
    • Ghosh, S., Marintcheva, B., Takahashi, M., and Richardson, C. C. (2009). C-terminal phenylalanine of bacteriophage T7 single-stranded DNA-binding protein is essential for strand displacement synthesis by T7 DNA polymerase at a nick in DNA. J. Biol. Chem. 284, 30339-30349. doi: 10.1074/jbc.M109.024059
    • (2009) J. Biol. Chem. , vol.284 , pp. 30339-30349
    • Ghosh, S.1    Marintcheva, B.2    Takahashi, M.3    Richardson, C.C.4
  • 12
    • 0015240411 scopus 로고
    • Deoxyribonucleic acid polymerase of bacteriophage T7
    • Grippo, P., and Richardson, C. C. (1971). Deoxyribonucleic acid polymerase of bacteriophage T7. J. Biol. Chem. 246, 6867-6873.
    • (1971) J. Biol. Chem. , vol.246 , pp. 6867-6873
    • Grippo, P.1    Richardson, C.C.2
  • 13
    • 34547740094 scopus 로고    scopus 로고
    • Dynamic DNA helicase-DNA polymerase interactions assure processive replication fork movement
    • doi: 10.1016/j.molcel.2007.06.020
    • Hamdan, S. M., Johnson, D. E., Tanner, N. A., Lee, J. B., Qimron, U., Tabor, S., et al. (2007). Dynamic DNA helicase-DNA polymerase interactions assure processive replication fork movement. Mol. Cell 27, 539-549. doi: 10.1016/j.molcel.2007.06.020
    • (2007) Mol. Cell , vol.27 , pp. 539-549
    • Hamdan, S.M.1    Johnson, D.E.2    Tanner, N.A.3    Lee, J.B.4    Qimron, U.5    Tabor, S.6
  • 14
    • 58249114971 scopus 로고    scopus 로고
    • Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis
    • doi: 10.1038/nature07512
    • Hamdan, S. M., Loparo, J. J., Takahashi, M., Richardson, C. C., and van Oijen, A. M. (2009). Dynamics of DNA replication loops reveal temporal control of lagging-strand synthesis. Nature 457, 336-339. doi: 10.1038/nature07512
    • (2009) Nature , vol.457 , pp. 336-339
    • Hamdan, S.M.1    Loparo, J.J.2    Takahashi, M.3    Richardson, C.C.4    van Oijen, A.M.5
  • 15
    • 17044382971 scopus 로고    scopus 로고
    • A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor
    • doi: 10.1073/pnas.0501637102
    • Hamdan, S. M., Marintcheva, B., Cook, T., Lee, S. J., Tabor, S., and Richardson, C. C. (2005). A unique loop in T7 DNA polymerase mediates the binding of helicase-primase, DNA binding protein, and processivity factor. Proc. Natl. Acad. Sci. U.S.A. 102, 5096-5101. doi: 10.1073/pnas.0501637102
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 5096-5101
    • Hamdan, S.M.1    Marintcheva, B.2    Cook, T.3    Lee, S.J.4    Tabor, S.5    Richardson, C.C.6
  • 16
    • 67650741773 scopus 로고    scopus 로고
    • Motors, switches, and contacts in the replisome
    • doi: 10.1146/annurev.biochem.78.072407.103248
    • Hamdan, S. M., and Richardson, C. C. (2009). Motors, switches, and contacts in the replisome. Annu. Rev. Biochem. 78, 205-243. doi: 10.1146/annurev.biochem.78.072407.103248
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 205-243
    • Hamdan, S.M.1    Richardson, C.C.2
  • 17
    • 0034889816 scopus 로고    scopus 로고
    • DNA polymerases as engines for biotechnology
    • Hamilton, S. C., Farchaus, J. W., and Davis, M. C. (2001). DNA polymerases as engines for biotechnology. Biotechniques 31, 370-376.
    • (2001) Biotechniques , vol.31 , pp. 370-376
    • Hamilton, S.C.1    Farchaus, J.W.2    Davis, M.C.3
  • 18
    • 0041529868 scopus 로고    scopus 로고
    • The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-binding protein modulates DNA binding and interaction with T7 DNA polymerase
    • doi: 10.1074/jbc.M304318200
    • He, Z. G., Rezende, L. F., Willcox, S., Griffith, J. D., and Richardson, C. C. (2003). The carboxyl-terminal domain of bacteriophage T7 single-stranded DNA-binding protein modulates DNA binding and interaction with T7 DNA polymerase. J. Biol. Chem. 278, 29538-29545. doi: 10.1074/jbc.M304318200
    • (2003) J. Biol. Chem. , vol.278 , pp. 29538-29545
    • He, Z.G.1    Rezende, L.F.2    Willcox, S.3    Griffith, J.D.4    Richardson, C.C.5
  • 20
    • 0018580360 scopus 로고
    • Deoxyribonucleic acid polymerase of bacteriophage T7. Characterization of the exonuclease activities of the gene 5 protein and the reconstituted polymerase
    • Hori, K., Mark, D. F., and Richardson, C. C. (1979a). Deoxyribonucleic acid polymerase of bacteriophage T7. Characterization of the exonuclease activities of the gene 5 protein and the reconstituted polymerase. J. Biol. Chem. 254, 11598-11604.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11598-11604
    • Hori, K.1    Mark, D.F.2    Richardson, C.C.3
  • 21
    • 0018610971 scopus 로고
    • Deoxyribonucleic acid polymerase of bacteriophage T7. Purification and properties of the phage-encoded subunit, the gene 5 protein
    • Hori, K., Mark, D. F., and Richardson, C. C. (1979b). Deoxyribonucleic acid polymerase of bacteriophage T7. Purification and properties of the phage-encoded subunit, the gene 5 protein. J. Biol. Chem. 254, 11591-11597.
    • (1979) J. Biol. Chem. , vol.254 , pp. 11591-11597
    • Hori, K.1    Mark, D.F.2    Richardson, C.C.3
  • 22
    • 0022999280 scopus 로고
    • Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity
    • Huber, H. E., Russel, M., Model, P., and Richardson, C. C. (1986). Interaction of mutant thioredoxins of Escherichia coli with the gene 5 protein of phage T7. The redox capacity of thioredoxin is not required for stimulation of DNA polymerase activity. J. Biol. Chem. 261, 15006-15012.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15006-15012
    • Huber, H.E.1    Russel, M.2    Model, P.3    Richardson, C.C.4
  • 23
    • 0023665337 scopus 로고
    • Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates
    • Huber, H. E., Tabor, S., and Richardson, C. C. (1987). Escherichia coli thioredoxin stabilizes complexes of bacteriophage T7 DNA polymerase and primed templates. J. Biol. Chem. 262, 16224-16232.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16224-16232
    • Huber, H.E.1    Tabor, S.2    Richardson, C.C.3
  • 24
    • 0038606491 scopus 로고    scopus 로고
    • A covalent linkage between the gene 5 DNA polymerase of bacteriophage T7 and Escherichia coli thioredoxin, the processivity factor: fate of thioredoxin during DNA synthesis
    • doi: 10.1074/jbc.M301366200
    • Johnson, D. E., and Richardson, C. C. (2003). A covalent linkage between the gene 5 DNA polymerase of bacteriophage T7 and Escherichia coli thioredoxin, the processivity factor: fate of thioredoxin during DNA synthesis. J. Biol. Chem. 278, 23762-23772. doi: 10.1074/jbc.M301366200
    • (2003) J. Biol. Chem. , vol.278 , pp. 23762-23772
    • Johnson, D.E.1    Richardson, C.C.2
  • 25
    • 34248327301 scopus 로고    scopus 로고
    • Exchange of DNA polymerases at the replication fork of bacteriophage T7
    • doi: 10.1073/pnas.0701062104
    • Johnson, D. E., Takahashi, M., Hamdan, S. M., Lee, S. J., and Richardson, C. C. (2007). Exchange of DNA polymerases at the replication fork of bacteriophage T7. Proc. Natl. Acad. Sci. U.S.A. 104, 5312-5317. doi: 10.1073/pnas.0701062104
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 5312-5317
    • Johnson, D.E.1    Takahashi, M.2    Hamdan, S.M.3    Lee, S.J.4    Richardson, C.C.5
  • 26
    • 84880693152 scopus 로고    scopus 로고
    • Genome of a SAR116 bacteriophage shows the prevalence of this phage type in the oceans
    • doi: 10.1073/pnas.1219930110
    • Kang, I., Oh, H. M., Kang, D., and Cho, J. C. (2013). Genome of a SAR116 bacteriophage shows the prevalence of this phage type in the oceans. Proc. Natl. Acad. Sci. U.S.A. 110, 12343-12348. doi: 10.1073/pnas.1219930110
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 12343-12348
    • Kang, I.1    Oh, H.M.2    Kang, D.3    Cho, J.C.4
  • 27
    • 84869049993 scopus 로고    scopus 로고
    • An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome
    • doi: 10.1074/jbc.M112.410647
    • Kulczyk, A. W., Akabayov, B., Lee, S. J., Bostina, M., Berkowitz, S. A., and Richardson, C. C. (2012). An interaction between DNA polymerase and helicase is essential for the high processivity of the bacteriophage T7 replisome. J. Biol. Chem. 287, 39050-39060. doi: 10.1074/jbc.M112.410647
    • (2012) J. Biol. Chem. , vol.287 , pp. 39050-39060
    • Kulczyk, A.W.1    Akabayov, B.2    Lee, S.J.3    Bostina, M.4    Berkowitz, S.A.5    Richardson, C.C.6
  • 28
    • 0032086491 scopus 로고    scopus 로고
    • Coordinated leading and lagging strand DNA synthesis on a minicircular template
    • doi: 10.1016/S1097-2765(00)80100-8
    • Lee, J., Chastain, P. D. 2nd, Kusakabe, T., Griffith, J. D., and Richardson, C. C. (1998). Coordinated leading and lagging strand DNA synthesis on a minicircular template. Mol. Cell 1, 1001-1010. doi: 10.1016/S1097-2765(00)80100-8
    • (1998) Mol. Cell , vol.1 , pp. 1001-1010
    • Lee, J.1    Chastain, P.D.2    Kusakabe, T.3    Griffith, J.D.4    Richardson, C.C.5
  • 29
    • 31844453991 scopus 로고    scopus 로고
    • DNA primase acts as a molecular brake in DNA replication
    • doi: 10.1038/nature04317
    • Lee, J. B., Hite, R. K., Hamdan, S. M., Xie, X. S., Richardson, C. C., and van Oijen, A. M. (2006). DNA primase acts as a molecular brake in DNA replication. Nature 439, 621-624. doi: 10.1038/nature04317
    • (2006) Nature , vol.439 , pp. 621-624
    • Lee, J.B.1    Hite, R.K.2    Hamdan, S.M.3    Xie, X.S.4    Richardson, C.C.5    van Oijen, A.M.6
  • 30
    • 27844554439 scopus 로고    scopus 로고
    • Mutability of DNA polymerase I: implications for the creation of mutant DNA polymerases
    • doi: 10.1016/j.dnarep.2005.09.006
    • Loh, E., and Loeb, L. A. (2005). Mutability of DNA polymerase I: implications for the creation of mutant DNA polymerases. DNA Repair (Amst.) 4, 1390-1398. doi: 10.1016/j.dnarep.2005.09.006
    • (2005) DNA Repair (Amst.) , vol.4 , pp. 1390-1398
    • Loh, E.1    Loeb, L.A.2
  • 31
    • 79952746781 scopus 로고    scopus 로고
    • Simultaneous single-molecule measurements of phage T7 replisome composition and function reveal the mechanism of polymerase exchange
    • doi: 10.1073/pnas.1018824108
    • Loparo, J. J., Kulczyk, A. W., Richardson, C. C., and van Oijen, A. M. (2011). Simultaneous single-molecule measurements of phage T7 replisome composition and function reveal the mechanism of polymerase exchange. Proc. Natl. Acad. Sci. U.S.A. 108, 3584-3589. doi: 10.1073/pnas.1018824108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 3584-3589
    • Loparo, J.J.1    Kulczyk, A.W.2    Richardson, C.C.3    van Oijen, A.M.4
  • 32
    • 0008062361 scopus 로고
    • Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase
    • doi: 10.1073/pnas.73.3.780
    • Mark, D. F., and Richardson, C. C. (1976). Escherichia coli thioredoxin: a subunit of bacteriophage T7 DNA polymerase. Proc. Natl. Acad. Sci. U.S.A. 73, 780-784. doi: 10.1073/pnas.73.3.780
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 780-784
    • Mark, D.F.1    Richardson, C.C.2
  • 33
    • 0016734786 scopus 로고
    • Bacteriophage T7 Deoxyribonucleic acid replication in vitro. A protein of Escherichia coli required for bacteriophage T7 DNA polymerase activity
    • Modrich, P., and Richardson, C. C. (1975a). Bacteriophage T7 Deoxyribonucleic acid replication in vitro. A protein of Escherichia coli required for bacteriophage T7 DNA polymerase activity. J. Biol. Chem. 250, 5508-5514.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5508-5514
    • Modrich, P.1    Richardson, C.C.2
  • 34
    • 0016733010 scopus 로고
    • Bacteriophage T7 deoxyribonucleic acid replication in vitro. Bacteriophage T7 DNA polymerase: an emzyme composed of phage-and host-specific subunits
    • Modrich, P., and Richardson, C. C. (1975b). Bacteriophage T7 deoxyribonucleic acid replication in vitro. Bacteriophage T7 DNA polymerase: an emzyme composed of phage-and host-specific subunits. J. Biol. Chem. 250, 5515-5522.
    • (1975) J. Biol. Chem. , vol.250 , pp. 5515-5522
    • Modrich, P.1    Richardson, C.C.2
  • 35
    • 72449204579 scopus 로고    scopus 로고
    • Coordinating DNA replication by means of priming loop and differential synthesis rate
    • doi: 10.1038/nature08611
    • Pandey, M., Syed, S., Donmez, I., Patel, G., Ha, T., and Patel, S. S. (2009). Coordinating DNA replication by means of priming loop and differential synthesis rate. Nature 462, 940-943. doi: 10.1038/nature08611
    • (2009) Nature , vol.462 , pp. 940-943
    • Pandey, M.1    Syed, S.2    Donmez, I.3    Patel, G.4    Ha, T.5    Patel, S.S.6
  • 36
    • 0035906661 scopus 로고    scopus 로고
    • Prokaryotic DNA polymerase I: evolution, structure, and "base flipping" mechanism for nucleotide selection
    • doi: 10.1006/jmbi.2001.4619
    • Patel, P. H., Suzuki, M., Adman, E., Shinkai, A., and Loeb, L. A. (2001). Prokaryotic DNA polymerase I: evolution, structure, and "base flipping" mechanism for nucleotide selection. J. Mol. Biol. 308, 823-837. doi: 10.1006/jmbi.2001.4619
    • (2001) J. Mol. Biol. , vol.308 , pp. 823-837
    • Patel, P.H.1    Suzuki, M.2    Adman, E.3    Shinkai, A.4    Loeb, L.A.5
  • 37
    • 34147098884 scopus 로고    scopus 로고
    • Genome sequence, structural proteins, and capsid organization of the cyanophage Syn5: a "horned" bacteriophage of marine Synechococcus
    • doi: 10.1016/j.jmb.2007.02.046
    • Pope, W. H., Weigele, P. R., Chang, J., Pedulla, M. L., Ford, M. E., Houtz, J. M., et al. (2007). Genome sequence, structural proteins, and capsid organization of the cyanophage Syn5: a "horned" bacteriophage of marine Synechococcus. J. Mol. Biol. 368, 966-981. doi: 10.1016/j.jmb.2007.02.046
    • (2007) J. Mol. Biol. , vol.368 , pp. 966-981
    • Pope, W.H.1    Weigele, P.R.2    Chang, J.3    Pedulla, M.L.4    Ford, M.E.5    Houtz, J.M.6
  • 38
    • 70349469948 scopus 로고    scopus 로고
    • Recent patents of gene sequences relative to DNA polymerases
    • doi: 10.2174/187221508786241729
    • Reha-Krantz, L. J. (2008). Recent patents of gene sequences relative to DNA polymerases. Recent Pat. DNA Gene Seq. 2, 145-163. doi: 10.2174/187221508786241729
    • (2008) Recent Pat. DNA Gene Seq. , vol.2 , pp. 145-163
    • Reha-Krantz, L.J.1
  • 39
    • 0020775545 scopus 로고
    • Bacteriophage T7: minimal requirements for the replication of a duplex DNA molecule
    • doi: 10.1016/0092-8674(83)90411-7
    • Richardson, C. C. (1983). Bacteriophage T7: minimal requirements for the replication of a duplex DNA molecule. Cell 33, 315-317. doi: 10.1016/0092-8674(83)90411-7
    • (1983) Cell , vol.33 , pp. 315-317
    • Richardson, C.C.1
  • 41
    • 84891166815 scopus 로고    scopus 로고
    • Shotgun metagenomics indicates novel family A DNA polymerases predominate within marine virioplankton
    • doi: 10.1038/ismej.2013.124
    • Schmidt, H. F., Sakowski, E. G., Williamson, S. J., Polson, S. W., and Wommack, K. E. (2014). Shotgun metagenomics indicates novel family A DNA polymerases predominate within marine virioplankton. ISME J. 8, 103-114. doi: 10.1038/ismej.2013.124
    • (2014) ISME J. , vol.8 , pp. 103-114
    • Schmidt, H.F.1    Sakowski, E.G.2    Williamson, S.J.3    Polson, S.W.4    Wommack, K.E.5
  • 42
    • 21344461027 scopus 로고    scopus 로고
    • Three Prochlorococcus cyanophage genomes: signature features and ecological interpretations
    • doi: 10.1371/journal.pbio.0030144
    • Sullivan, M. B., Coleman, M. L., Weigele, P., Rohwer, F., and Chisholm, S. W. (2005). Three Prochlorococcus cyanophage genomes: signature features and ecological interpretations. PLoS Biol. 3:e144. doi: 10.1371/journal.pbio.0030144
    • (2005) PLoS Biol. , vol.3
    • Sullivan, M.B.1    Coleman, M.L.2    Weigele, P.3    Rohwer, F.4    Chisholm, S.W.5
  • 43
    • 25144506135 scopus 로고    scopus 로고
    • Viruses in the sea
    • doi: 10.1038/nature04160
    • Suttle, C. A. (2005). Viruses in the sea. Nature 437, 356-361. doi: 10.1038/nature04160
    • (2005) Nature , vol.437 , pp. 356-361
    • Suttle, C.A.1
  • 44
    • 0024596736 scopus 로고
    • Selective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis
    • Tabor, S., and Richardson, C. C. (1989a). Selective inactivation of the exonuclease activity of bacteriophage T7 DNA polymerase by in vitro mutagenesis. J. Biol. Chem. 264, 6447-6458.
    • (1989) J. Biol. Chem. , vol.264 , pp. 6447-6458
    • Tabor, S.1    Richardson, C.C.2
  • 45
    • 0006962619 scopus 로고
    • Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I
    • doi: 10.1073/pnas.86.11.4076
    • Tabor, S., and Richardson, C. C. (1989b). Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I. Proc. Natl. Acad. Sci. U.S.A. 86, 4076-4080. doi: 10.1073/pnas.86.11.4076
    • (1989) Proc. Natl. Acad. Sci. U.S.A. , vol.86 , pp. 4076-4080
    • Tabor, S.1    Richardson, C.C.2
  • 46
    • 0025317061 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Effect of pyrophosphorolysis and metal ions
    • Tabor, S., and Richardson, C. C. (1990). DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Effect of pyrophosphorolysis and metal ions. J. Biol. Chem. 265, 8322-8328.
    • (1990) J. Biol. Chem. , vol.265 , pp. 8322-8328
    • Tabor, S.1    Richardson, C.C.2
  • 47
    • 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
    • doi: 10.1073/pnas.92.14.6339
    • Tabor, S., and Richardson, C. C. (1995). 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, 6339-6343. doi: 10.1073/pnas.92.14.6339
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6339-6343
    • Tabor, S.1    Richardson, C.C.2
  • 48
    • 0023665251 scopus 로고
    • Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7
    • Tabor, S., Huber, H. E., and Richardson, C. C. (1987a). Escherichia coli thioredoxin confers processivity on the DNA polymerase activity of the gene 5 protein of bacteriophage T7. J. Biol. Chem. 262, 16212-16223.
    • (1987) J. Biol. Chem. , vol.262 , pp. 16212-16223
    • Tabor, S.1    Huber, H.E.2    Richardson, C.C.3
  • 49
    • 0023656972 scopus 로고
    • Selective oxidation of the exonuclease domain of bacteriophage T7 DNA polymerase
    • Tabor, S., and Richardson, C. C. (1987b). Selective oxidation of the exonuclease domain of bacteriophage T7 DNA polymerase. J. Biol. Chem. 262, 15330-15333.
    • (1987) J. Biol. Chem. , vol.262 , pp. 15330-15333
    • Tabor, S.1    Richardson, C.C.2
  • 50
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • doi: 10.1073/pnas.84.14.4767
    • Tabor, S., and Richardson, C. C. (1987c). DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc. Natl. Acad. Sci. U.S.A. 84, 4767-4771. doi: 10.1073/pnas.84.14.4767
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 51
    • 84869233533 scopus 로고    scopus 로고
    • Thioredoxin, the processivity factor, sequesters an exposed cysteine in the thumb domain of bacteriophage T7 DNA polymerase
    • doi: 10.1074/jbc.M112.409235
    • Tran, N. Q., Lee, S. J., Akabayov, B., Johnson, D. E., and Richardson, C. C. (2012). Thioredoxin, the processivity factor, sequesters an exposed cysteine in the thumb domain of bacteriophage T7 DNA polymerase. J. Biol. Chem. 287, 39732-39741. doi: 10.1074/jbc.M112.409235
    • (2012) J. Biol. Chem. , vol.287 , pp. 39732-39741
    • Tran, N.Q.1    Lee, S.J.2    Akabayov, B.3    Johnson, D.E.4    Richardson, C.C.5
  • 52
    • 79959357956 scopus 로고    scopus 로고
    • Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis
    • doi: 10.1073/pnas.1106678108
    • Zhang, H., Lee, S. J., Zhu, B., Tran, N. Q., Tabor, S., and Richardson, C. C. (2011). Helicase-DNA polymerase interaction is critical to initiate leading-strand DNA synthesis. Proc. Natl. Acad. Sci. U.S.A. 108, 9372-9377. doi: 10.1073/pnas.1106678108
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 9372-9377
    • Zhang, H.1    Lee, S.J.2    Zhu, B.3    Tran, N.Q.4    Tabor, S.5    Richardson, C.C.6
  • 53
    • 77952704134 scopus 로고    scopus 로고
    • Direct role for the RNA polymerase domain of T7 primase in primer delivery
    • doi: 10.1073/pnas.1004220107
    • Zhu, B., Lee, S. J., and Richardson, C. C. (2010). Direct role for the RNA polymerase domain of T7 primase in primer delivery. Proc. Natl. Acad. Sci. U.S.A. 107, 9099-9104. doi: 10.1073/pnas.1004220107
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 9099-9104
    • Zhu, B.1    Lee, S.J.2    Richardson, C.C.3
  • 54
    • 80051493716 scopus 로고    scopus 로고
    • Bypass of a nick by the replisome of bacteriophage T7
    • doi: 10.1074/jbc.M111.252023
    • Zhu, B., Lee, S. J., and Richardson, C. C. (2011). Bypass of a nick by the replisome of bacteriophage T7. J. Biol. Chem. 286, 28488-28497. doi: 10.1074/jbc.M111.252023
    • (2011) J. Biol. Chem. , vol.286 , pp. 28488-28497
    • Zhu, B.1    Lee, S.J.2    Richardson, C.C.3
  • 56
    • 84898998425 scopus 로고    scopus 로고
    • Syn5 RNA polymerase synthesizes precise run-off RNA products
    • doi: 10.1093/nar/gkt1193
    • Zhu, B., Tabor, S., and Richardson, C. C. (2013b). Syn5 RNA polymerase synthesizes precise run-off RNA products. Nucleic Acids Res. 42:e33. doi: 10.1093/nar/gkt1193
    • (2013) Nucleic Acids Res. , vol.42
    • Zhu, B.1    Tabor, S.2    Richardson, C.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.