메뉴 건너뛰기




Volumn 278, Issue 1, 1998, Pages 147-165

How E. Coli DNA polymerase I (Klenow fragment) distinguishes between deoxy- and dideoxynucleotides

Author keywords

Chain terminator; Dideoxynucleotide; DNA polymerase I; dNTP binding site; Klenow fragment

Indexed keywords

DEOXYRIBONUCLEOTIDE; DNA DIRECTED DNA POLYMERASE BETA;

EID: 0032562549     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1672     Document Type: Article
Times cited : (99)

References (79)
  • 1
    • 0026459950 scopus 로고
    • Molecular cloning and nucleotide sequence of the DNA polymerase gene from Thermus flavus
    • Akhmetzjanov A.A., Vakhitov V.A. Molecular cloning and nucleotide sequence of the DNA polymerase gene from Thermus flavus. Nucl. Acids Res. 20:1992;5839
    • (1992) Nucl. Acids Res. , vol.20 , pp. 5839
    • Akhmetzjanov, A.A.1    Vakhitov, V.A.2
  • 2
    • 0027483668 scopus 로고
    • Cloning, nucleotide sequence, and expression in Escherichia coli of DNA polymerase gene (polA) from Thermus thermophilus hb8
    • Asakura K., Komatsubara H., Soga S., Yomo T., Oka M., Emi S., Urabe I. Cloning, nucleotide sequence, and expression in Escherichia coli of DNA polymerase gene (polA) from Thermus thermophilus hb8. J. Ferment. Bioeng. 76:1993;265-269
    • (1993) J. Ferment. Bioeng. , vol.76 , pp. 265-269
    • Asakura, K.1    Komatsubara, H.2    Soga, S.3    Yomo, T.4    Oka, M.5    Emi, S.6    Urabe, I.7
  • 3
    • 0028947982 scopus 로고
    • 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. Deoxynucleoside triphosphate and pyrophosphate binding sites in the catalytically competent ternary complex for the polymerase reaction catalyzed by DNA polymerase I (Klenow fragment). J. Biol. Chem. 270:1995;1945-1954
    • (1995) J. Biol. Chem. , vol.270 , pp. 1945-1954
    • Astatke, M.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 4
    • 0032584219 scopus 로고    scopus 로고
    • A single side-chain prevents E. coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides
    • in the press
    • Astatke M., Ng K., Grindley N.D.F., Joyce C.M. A single side-chain prevents E. coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides. Proc. Natl Acad. Sci. USA. 1998;. in the press
    • (1998) Proc. Natl Acad. Sci. USA
    • Astatke, M.1    Ng, K.2    Grindley, N.D.F.3    Joyce, C.M.4
  • 5
    • 0014619339 scopus 로고
    • Enzymatic synthesis of deoxyribonucleic acid. XXXIV. Termination of chain growth by a 2′,3′-dideoxy ribonucleotide
    • Atkinson M.R., Deutscher M.P., Kornberg A., Russell A.F., Moffatt J.G. Enzymatic synthesis of deoxyribonucleic acid. XXXIV. Termination of chain growth by a 2′,3′-dideoxy ribonucleotide. Biochemistry. 8:1969;4897-4904
    • (1969) Biochemistry , vol.8 , pp. 4897-4904
    • Atkinson, M.R.1    Deutscher, M.P.2    Kornberg, A.3    Russell, A.F.4    Moffatt, J.G.5
  • 6
    • 0024819291 scopus 로고
    • Sequence of bacteriophage T3 DNA from gene 2. 5 through gene 9
    • Beck P.J., Gonzalez S., Ward C.L., Molineux I.J. Sequence of bacteriophage T3 DNA from gene 2. 5 through gene 9. J. Mol. Biol. 210:1989;687-701
    • (1989) J. Mol. Biol. , vol.210 , pp. 687-701
    • Beck, P.J.1    Gonzalez, S.2    Ward, C.L.3    Molineux, I.J.4
  • 7
    • 0026019625 scopus 로고
    • Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I: A two metal ion mechanism
    • Beese L.S., Steitz T.A. Structural basis for the 3′-5′ exonuclease activity of Escherichia coli DNA polymerase I a two metal ion mechanism. EMBO J. 10:1991;25-33
    • (1991) EMBO J. , vol.10 , pp. 25-33
    • Beese, L.S.1    Steitz, T.A.2
  • 8
    • 0027231782 scopus 로고
    • Structure of DNA polymerase I Klenow fragment bound to duplex DNA
    • Beese L.S., Derbyshire V., Steitz T.A. Structure of DNA polymerase I Klenow fragment bound to duplex DNA. Science. 260:1993;352-355
    • (1993) Science , vol.260 , pp. 352-355
    • Beese, L.S.1    Derbyshire, V.2    Steitz, T.A.3
  • 9
    • 0027730441 scopus 로고
    • Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate
    • Beese L.S., Friedman J.M., Steitz T.A. Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate. Biochemistry. 32:1993;14095-14101
    • (1993) Biochemistry , vol.32 , pp. 14095-14101
    • Beese, L.S.1    Friedman, J.M.2    Steitz, T.A.3
  • 10
    • 0030906056 scopus 로고    scopus 로고
    • Base miscoding and strand misalignment errors by mutator 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. Base miscoding and strand misalignment errors by mutator polymerases with amino acid substitutions at tyrosine 766 in the O helix of the fingers subdomain. J. Biol. Chem. 272:1997;7345-7351
    • (1997) J. Biol. Chem. , vol.272 , pp. 7345-7351
    • Bell, J.B.1    Eckert, K.A.2    Joyce, C.M.3    Kunkel, T.A.4
  • 11
    • 0027217643 scopus 로고
    • Compilation, alignment, and phylogenetic relationships of DNA polymerases
    • Braithwaite D.K., Ito J. Compilation, alignment, and phylogenetic relationships of DNA polymerases. Nucl. Acids Res. 21:1993;787-802
    • (1993) Nucl. Acids Res. , vol.21 , pp. 787-802
    • Braithwaite, D.K.1    Ito, J.2
  • 12
    • 0030051173 scopus 로고    scopus 로고
    • Slow rate of phosphodiester bond formation accounts for the strong bias that Taq DNA poly merase shows against 2′,3′-dideoxynucleotide terminators
    • Brandis J.W., Edwards S.G., Johnson K.A. Slow rate of phosphodiester bond formation accounts for the strong bias that Taq DNA poly merase shows against 2′,3′-dideoxynucleotide terminators. Biochemistry. 35:1996;2189-2200
    • (1996) Biochemistry , vol.35 , pp. 2189-2200
    • Brandis, J.W.1    Edwards, S.G.2    Johnson, K.A.3
  • 13
    • 0023110653 scopus 로고
    • Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine
    • Brick P., Blow D.M. Crystal structure of a deletion mutant of a tyrosyl-tRNA synthetase complexed with tyrosine. J. Mol. Biol. 194:1987;287-297
    • (1987) J. Mol. Biol. , vol.194 , pp. 287-297
    • Brick, P.1    Blow, D.M.2
  • 15
    • 0021107939 scopus 로고
    • Elementary steps in the DNA polymerase I reaction pathway
    • Bryant F.R., Johnson K.A., Benkovic S.J. Elementary steps in the DNA polymerase I reaction pathway. Biochemistry. 22:1983;3537-3546
    • (1983) Biochemistry , vol.22 , pp. 3537-3546
    • Bryant, F.R.1    Johnson, K.A.2    Benkovic, S.J.3
  • 16
    • 0018287755 scopus 로고
    • A study of the mechanism of DNA polymerase I from Escherichia coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate
    • Burgers P.M.J., Eckstein F. A study of the mechanism of DNA polymerase I from Escherichia coli with diastereomeric phosphorothioate analogs of deoxyadenosine triphosphate. J. Biol. Chem. 254:1979;6889-6893
    • (1979) J. Biol. Chem. , vol.254 , pp. 6889-6893
    • Burgers, P.M.J.1    Eckstein, F.2
  • 17
    • 0026029379 scopus 로고
    • A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity
    • Carroll S.S., Cowart M., Benkovic S.J. A mutant of DNA polymerase I (Klenow fragment) with reduced fidelity. Biochemistry. 30:1991;804-813
    • (1991) Biochemistry , vol.30 , pp. 804-813
    • Carroll, S.S.1    Cowart, M.2    Benkovic, S.J.3
  • 18
    • 0025799903 scopus 로고
    • Kinetic mechanism of DNA polymerase I (Klenow fragment) identification of a second conformational change and evaluation of the internal equilibrium constant
    • Dahlberg M.E., Benkovic S.J. Kinetic mechanism of DNA polymerase I (Klenow fragment) identification of a second conformational change and evaluation of the internal equilibrium constant. Biochemistry. 30:1991;4835-4843
    • (1991) Biochemistry , vol.30 , pp. 4835-4843
    • Dahlberg, M.E.1    Benkovic, S.J.2
  • 21
    • 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 N.D.F., Joyce C.M. 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. 10:1991;17-24
    • (1991) EMBO J. , vol.10 , pp. 17-24
    • Derbyshire, V.1    Grindley, N.D.F.2    Joyce, C.M.3
  • 22
    • 0028564813 scopus 로고
    • Mutants affecting nucleotide recognition by T7 DNA polymerase
    • Donlin M.J., Johnson K.A. Mutants affecting nucleotide recognition by T7 DNA polymerase. Biochemistry. 33:1994;14908-14917
    • (1994) Biochemistry , vol.33 , pp. 14908-14917
    • Donlin, M.J.1    Johnson, K.A.2
  • 23
    • 0032518398 scopus 로고    scopus 로고
    • 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. 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
    • Doublié, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 24
    • 0020964297 scopus 로고
    • Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements
    • Dunn J.J., Studier F.W. Complete nucleotide sequence of bacteriophage T7 DNA and the locations of T7 genetic elements. J. Mol. Biol. 166:1983;477-535
    • (1983) J. Mol. Biol. , vol.166 , pp. 477-535
    • Dunn, J.J.1    Studier, F.W.2
  • 25
    • 0030746339 scopus 로고    scopus 로고
    • Characterization of Lactococcus lactis UV-sensitive mutants obtained by ISS1 transposition
    • Duwat P., Cochu A., Ehrlich S.D., Gruss A. Characterization of Lactococcus lactis UV-sensitive mutants obtained by ISS1 transposition. J. Bacteriol. 179:1997;4473-4479
    • (1997) J. Bacteriol. , vol.179 , pp. 4473-4479
    • Duwat, P.1    Cochu, A.2    Ehrlich, S.D.3    Gruss, A.4
  • 27
    • 0022893858 scopus 로고
    • NMR studies of conformations and interactions of substrates and ribonucleotide templates bound to the large fragment of DNA polymerase I
    • Ferrin L.J., Mildvan A.S. NMR studies of conformations and interactions of substrates and ribonucleotide templates bound to the large fragment of DNA polymerase I. Biochemistry. 25:1986;5131-5145
    • (1986) Biochemistry , vol.25 , pp. 5131-5145
    • Ferrin, L.J.1    Mildvan, A.S.2
  • 30
    • 0024306516 scopus 로고
    • Cloning and sequencing of the nuclear gene MIP1 encoding the catalytic subunit of the yeast mitochondrial DNA polymerase
    • Foury F. Cloning and sequencing of the nuclear gene MIP1 encoding the catalytic subunit of the yeast mitochondrial DNA polymerase. J. Biol. Chem. 264:1989;20552-20560
    • (1989) J. Biol. Chem. , vol.264 , pp. 20552-20560
    • Foury, F.1
  • 31
    • 0022965458 scopus 로고
    • A domain of the Klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity
    • Freemont P.S., Ollis D.L., Steitz T.A., Joyce C.M. A domain of the Klenow fragment of Escherichia coli DNA polymerase I has polymerase but no exonuclease activity. Proteins: Struct. Funct. Genet. 1:1986;66-73
    • (1986) Proteins: Struct. Funct. Genet. , vol.1 , pp. 66-73
    • Freemont, P.S.1    Ollis, D.L.2    Steitz, T.A.3    Joyce, C.M.4
  • 33
    • 0027262177 scopus 로고
    • Identification, sequencing, and targeted mutagenesis of a DNA polymerase gene required for the extreme radioresistance of Deinococcus radiodurans
    • Gutman P.D., Fuchs P., Ouyang L., Minton K.W. Identification, sequencing, and targeted mutagenesis of a DNA polymerase gene required for the extreme radioresistance of Deinococcus radiodurans. J. Bacteriol. 175:1993;3581-3590
    • (1993) J. Bacteriol. , vol.175 , pp. 3581-3590
    • Gutman, P.D.1    Fuchs, P.2    Ouyang, L.3    Minton, K.W.4
  • 34
    • 0029789574 scopus 로고    scopus 로고
    • Molecular cloning of Drosophila mus308, a gene involved in DNA cross-link repair with homology to prokaryotic DNA polymerase I genes
    • Harris P.V., Mazina O.M., Leonhardt E.A., Case R.B., Boyd J.B., Burtis K.C. Molecular cloning of Drosophila mus308, a gene involved in DNA cross-link repair with homology to prokaryotic DNA polymerase I genes. Mol. Cell. Biol. 16:1996;5764-5771
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5764-5771
    • Harris, P.V.1    Mazina, O.M.2    Leonhardt, E.A.3    Case, R.B.4    Boyd, J.B.5    Burtis, K.C.6
  • 35
    • 0028110883 scopus 로고
    • Sequence of the essential early region of phi C31, a temperate phage of Streptomyces spp. with unusual features in its lytic development
    • Hartley N.M., Murphy G.O., Bruton C.J., Chater K.F. Sequence of the essential early region of phi C31, a temperate phage of Streptomyces spp. with unusual features in its lytic development. Gene. 147:1994;29-40
    • (1994) Gene , vol.147 , pp. 29-40
    • Hartley, N.M.1    Murphy, G.O.2    Bruton, C.J.3    Chater, K.F.4
  • 36
    • 0027456546 scopus 로고
    • DNA sequence, structure and gene expression of mycobacteriophage L5: A phage system for mycobacterial genetics
    • Hatfull G.F., Sarkis G.J. DNA sequence, structure and gene expression of mycobacteriophage L5 a phage system for mycobacterial genetics. Mol. Microbiol. 7:1993;395-405
    • (1993) Mol. Microbiol. , vol.7 , pp. 395-405
    • Hatfull, G.F.1    Sarkis, G.J.2
  • 37
    • 0030854581 scopus 로고    scopus 로고
    • Mechanism of ribose 2′-group discrimination by an RNA polymerase
    • Huang Y., Eckstein F., Padilla R., Sousa R. Mechanism of ribose 2′-group discrimination by an RNA polymerase. Biochemistry. 36:1997;8231-8242
    • (1997) Biochemistry , vol.36 , pp. 8231-8242
    • Huang, Y.1    Eckstein, F.2    Padilla, R.3    Sousa, R.4
  • 38
    • 0028820249 scopus 로고
    • Cloning and sequence analysis of the gene encoding the DNA polymerase I from Mycobacterium tuberculosis
    • Huberts P., Mizrahi V. Cloning and sequence analysis of the gene encoding the DNA polymerase I from Mycobacterium tuberculosis. Gene. 164:1995;133-136
    • (1995) Gene , vol.164 , pp. 133-136
    • Huberts, P.1    Mizrahi, V.2
  • 39
    • 0025925048 scopus 로고
    • 1-H NMR study of the sugar pucker of 2′,3′-dideoxynucleosides with anti-human immunodeficiencey virus (HIV) activity
    • Jagannadh B., Reedy D.V., Kunwar A.C. 1-H NMR study of the sugar pucker of 2′,3′-dideoxynucleosides with anti-human immunodeficiencey virus (HIV) activity. Biochem. Biophys. Res. Commun. 179:1991;386-391
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 386-391
    • Jagannadh, B.1    Reedy, D.V.2    Kunwar, A.C.3
  • 40
    • 0028916224 scopus 로고
    • Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates
    • Johnson K.A. Rapid quench kinetic analysis of polymerases, adenosinetriphosphatases, and enzyme intermediates. Methods Enzymol. 249:1995;38-61
    • (1995) Methods Enzymol. , vol.249 , pp. 38-61
    • Johnson, K.A.1
  • 41
    • 0031042722 scopus 로고    scopus 로고
    • Choosing the right sugar: How polymerases select a nucleotide substrate
    • Joyce C.M. Choosing the right sugar how polymerases select a nucleotide substrate. Proc. Natl Acad. Sci. USA. 94:1997;1619-1622
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 1619-1622
    • Joyce, C.M.1
  • 42
    • 0028827318 scopus 로고
    • Purification of E. coli DNA polymerase I and Klenow fragment
    • Joyce C.M., Derbyshire V. Purification of E. coli DNA polymerase I and Klenow fragment. Methods Enzymol. 262:1994;3-13
    • (1994) Methods Enzymol. , vol.262 , pp. 3-13
    • Joyce, C.M.1    Derbyshire, V.2
  • 43
    • 0028206048 scopus 로고
    • Function and structure relationships in DNA polymerases
    • Joyce C.M., Steitz T.A. Function and structure relationships in DNA polymerases. Annu. Rev. Biochem. 63:1994;777-822
    • (1994) Annu. Rev. Biochem. , vol.63 , pp. 777-822
    • Joyce, C.M.1    Steitz, T.A.2
  • 44
    • 0028881713 scopus 로고
    • Polymerase structures and function: Variations on a theme
    • Joyce C.M., Steitz T.A. Polymerase structures and function variations on a theme. J. Bacteriol. 177:1995;6321-6329
    • (1995) J. Bacteriol. , vol.177 , pp. 6321-6329
    • Joyce, C.M.1    Steitz, T.A.2
  • 45
    • 0020490301 scopus 로고
    • Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I
    • Joyce C.M., Kelley W.S., Grindley N.D.F. Nucleotide sequence of the Escherichia coli polA gene and primary structure of DNA polymerase I. J. Biol. Chem. 257:1982;1958-1964
    • (1982) J. Biol. Chem. , vol.257 , pp. 1958-1964
    • Joyce, C.M.1    Kelley, W.S.2    Grindley, N.D.F.3
  • 46
    • 0029655167 scopus 로고
    • Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome
    • Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., Sugiura M., Tabata S. Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region from map positions 64% to 92% of the genome. DNA Res. 2:1995;153-166
    • (1995) DNA Res. , vol.2 , pp. 153-166
    • Kaneko, T.1    Tanaka, A.2    Sato, S.3    Kotani, H.4    Sazuka, T.5    Miyajima, N.6    Sugiura, M.7    Tabata, S.8
  • 47
    • 0029894752 scopus 로고    scopus 로고
    • Significance of the O-helix residues of Escherichia coli DNA polymerase I in DNA synthesis: Dynamics of the dNTP binding pocket
    • Kaushik N., Pandey V.N., Modak M.J. Significance of the O-helix residues of Escherichia coli DNA polymerase I in DNA synthesis dynamics of the dNTP binding pocket. Biochemistry. 35:1996;7256-7266
    • (1996) Biochemistry , vol.35 , pp. 7256-7266
    • Kaushik, N.1    Pandey, V.N.2    Modak, M.J.3
  • 48
    • 0014708426 scopus 로고
    • Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis
    • Klenow H., Henningsen I. Selective elimination of the exonuclease activity of the deoxyribonucleic acid polymerase from Escherichia coli B by limited proteolysis. Proc. Natl Acad. Sci. USA. 65:1970;168-175
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 168-175
    • Klenow, H.1    Henningsen, I.2
  • 49
    • 0026693137 scopus 로고
    • Crystal structure at 3.5 a resolution of HIV-1 reverse transcriptase complexed with an inhibitor
    • Kohlstaedt L.A., Wang J., Friedman J.M., Rice P.A., Steitz T.A. Crystal structure at 3.5 A resolution of HIV-1 reverse transcriptase complexed with an inhibitor. Science. 256:1992;1783-1790
    • (1992) Science , vol.256 , pp. 1783-1790
    • Kohlstaedt, L.A.1    Wang, J.2    Friedman, J.M.3    Rice, P.A.4    Steitz, T.A.5
  • 51
    • 0030690274 scopus 로고    scopus 로고
    • Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region
    • Lapidus A., Galleron N., Sorokin A., Ehrlich S.D. Sequencing and functional annotation of the Bacillus subtilis genes in the 200 kb rrnB-dnaB region. Microbiology. 143:1997;3431-3441
    • (1997) Microbiology , vol.143 , pp. 3431-3441
    • Lapidus, A.1    Galleron, N.2    Sorokin, A.3    Ehrlich, S.D.4
  • 52
    • 0024560060 scopus 로고
    • Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus
    • Lawyer F.C., Stoffel S., Saiki R.K., Myambo K., Drummond R., Gelfand D.H. Isolation, characterization, and expression in Escherichia coli of the DNA polymerase gene from Thermus aquaticus. J. Biol. Chem. 264:1989;6427-6437
    • (1989) J. Biol. Chem. , vol.264 , pp. 6427-6437
    • Lawyer, F.C.1    Stoffel, S.2    Saiki, R.K.3    Myambo, K.4    Drummond, R.5    Gelfand, D.H.6
  • 53
    • 0024380989 scopus 로고
    • T5 DNA polymerase: Structural-functional relationships to other DNA polymerases
    • Leavitt M.C., Ito J. T5 DNA polymerase structural-functional relationships to other DNA polymerases. Proc. Natl Acad. Sci. USA. 86:1989;4465-4469
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4465-4469
    • Leavitt, M.C.1    Ito, J.2
  • 54
    • 0024557063 scopus 로고
    • Characterization of the polA gene of Streptococcus pneumoniae and comparison of the DNA polymerase I it encodes to homologous enzymes from Escherichia coli and phage T7
    • Lopez P., Martinez S., Diaz A., Espinosa M., Lacks S.A. Characterization of the polA gene of Streptococcus pneumoniae and comparison of the DNA polymerase I it encodes to homologous enzymes from Escherichia coli and phage T7. J. Biol. Chem. 264:1989;4255-4263
    • (1989) J. Biol. Chem. , vol.264 , pp. 4255-4263
    • Lopez, P.1    Martinez, S.2    Diaz, A.3    Espinosa, M.4    Lacks, S.A.5
  • 55
    • 0025186450 scopus 로고
    • Molecular targets for AIDS therapy
    • Mitsuya H., Yarchoan R., Broder S. Molecular targets for AIDS therapy. Science. 249:1990;1533-1543
    • (1990) Science , vol.249 , pp. 1533-1543
    • Mitsuya, H.1    Yarchoan, R.2    Broder, S.3
  • 56
    • 0030444635 scopus 로고    scopus 로고
    • Deoxy- and dideoxynucleotide discrimination and identification of critical 5′ nuclease domain residues of the DNA polymerase I from Mycobacterium tuberculosis
    • Mizrahi V., Huberts P. Deoxy- and dideoxynucleotide discrimination and identification of critical 5′ nuclease domain residues of the DNA polymerase I from Mycobacterium tuberculosis. Nucl. Acids Res. 24:1996;4845-4852
    • (1996) Nucl. Acids Res. , vol.24 , pp. 4845-4852
    • Mizrahi, V.1    Huberts, P.2
  • 57
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., Honig B. Protein folding and association insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins: Struct. Funct. Genet. 11:1991;281-296
    • (1991) Proteins: Struct. Funct. Genet. , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 58
    • 0021984004 scopus 로고
    • Structure of large fragment of Escherichia coli DNA polymerase I complexed with dTMP
    • Ollis D.L., Brick P., Hamlin R., Xuong N.G., Steitz T.A. 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    Brick, P.2    Hamlin, R.3    Xuong, N.G.4    Steitz, T.A.5
  • 59
    • 0028338541 scopus 로고
    • Role of lysine 758 of Escherichia coli DNA polymerase I as assessed by site-directed mutagenesis
    • Pandey V.N., Kaushik N., Modak M.J. Role of lysine 758 of Escherichia coli DNA polymerase I as assessed by site-directed mutagenesis. J. Biol. Chem. 269:1994;13259-13265
    • (1994) J. Biol. Chem. , vol.269 , pp. 13259-13265
    • Pandey, V.N.1    Kaushik, N.2    Modak, M.J.3
  • 60
    • 0025121103 scopus 로고
    • 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. Identification of residues critical for the polymerase activity of the Klenow fragment of DNA polymerase I from Escherichia coli. J. Biol. Chem. 265:1990;14579-14591
    • (1990) J. Biol. Chem. , vol.265 , pp. 14579-14591
    • Polesky, A.H.1    Steitz, T.A.2    Grindley, N.D.F.3    Joyce, C.M.4
  • 61
    • 0026713678 scopus 로고
    • 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. Side-chains involved in catalysis of the polymerase reaction of DNA polymerase I from Escherichia coli. J. Biol. Chem. 267:1992;8417-8428
    • (1992) J. Biol. Chem. , vol.267 , pp. 8417-8428
    • Polesky, A.H.1    Dahlberg, M.E.2    Benkovic, S.J.3    Grindley, N.D.F.4    Joyce, C.M.5
  • 62
    • 0001339532 scopus 로고
    • A program to produce both detailed and schematic drawings for protein structures
    • Priestle J.P. A program to produce both detailed and schematic drawings for protein structures. J. Appl. Crystallog. 24:1991;946-950
    • (1991) J. Appl. Crystallog. , vol.24 , pp. 946-950
    • Priestle, J.P.1
  • 63
    • 0024804759 scopus 로고
    • Absorbance melting curves of RNA
    • Puglisi J.D., Tinoco I. Absorbance melting curves of RNA. Methods Enzymol. 180:1989;304-325
    • (1989) Methods Enzymol. , vol.180 , pp. 304-325
    • Puglisi, J.D.1    Tinoco, I.2
  • 64
    • 0021147979 scopus 로고
    • Nucleotide sequence of the temperate Bacillus subtilis bacteriophage SP02 DNA polymerase gene L
    • Raden B., Rutberg L. Nucleotide sequence of the temperate Bacillus subtilis bacteriophage SP02 DNA polymerase gene L. J. Virol. 52:1984;9-15
    • (1984) J. Virol. , vol.52 , pp. 9-15
    • Raden, B.1    Rutberg, L.2
  • 65
    • 0029943569 scopus 로고    scopus 로고
    • Construction of single amino acid substitution mutants of cloned Bacillus stearothermophilus DNA polymerase I which lack 5′→3′ exonuclease activity
    • Riggs M.G., Tudor S., Sivaram M., McDonough S.H. Construction of single amino acid substitution mutants of cloned Bacillus stearothermophilus DNA polymerase I which lack 5′→3′ exonuclease activity. Biochim. Biophys. Acta. 1307:1996;178-186
    • (1996) Biochim. Biophys. Acta , vol.1307 , pp. 178-186
    • Riggs, M.G.1    Tudor, S.2    Sivaram, M.3    McDonough, S.H.4
  • 68
    • 0026782560 scopus 로고
    • The DNA polymerase-encoding gene of Bacillus subtilis bacteriophage SP01
    • Scarlato V., Gargano S. The DNA polymerase-encoding gene of Bacillus subtilis bacteriophage SP01. Gene. 118:1992;109-113
    • (1992) Gene , vol.118 , pp. 109-113
    • Scarlato, V.1    Gargano, S.2
  • 69
    • 0016817216 scopus 로고
    • Conformation of deoxynucleoside triphosphate substrates on DNA polymerase I from Escherichia coli as determined by nuclear magnetic relaxation
    • Sloan D.L., Loeb L.A., Mildvan A.S. Conformation of deoxynucleoside triphosphate substrates on DNA polymerase I from Escherichia coli as determined by nuclear magnetic relaxation. J. Biol. Chem. 250:1975;8913-8920
    • (1975) J. Biol. Chem. , vol.250 , pp. 8913-8920
    • Sloan, D.L.1    Loeb, L.A.2    Mildvan, A.S.3
  • 70
    • 0029091457 scopus 로고
    • A mutant T7 RNA polymerase as a DNA polymerase
    • Sousa R., Padilla R. A mutant T7 RNA polymerase as a DNA polymerase. EMBO J. 14:1995;4609-4621
    • (1995) EMBO J. , vol.14 , pp. 4609-4621
    • Sousa, R.1    Padilla, R.2
  • 71
    • 0027163526 scopus 로고
    • Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution
    • Sousa R., Chung Y.J., Rose J.P., Wang B.C. Crystal structure of bacteriophage T7 RNA polymerase at 3.3 Å resolution. Nature. 364:1993;593-599
    • (1993) Nature , vol.364 , pp. 593-599
    • Sousa, R.1    Chung, Y.J.2    Rose, J.P.3    Wang, B.C.4
  • 72
    • 0029845979 scopus 로고    scopus 로고
    • Random mutagenesis of Thermus aquaticus DNA polymerase I: Concordance of immutable sites in vivo with the crystal structure
    • Suzuki M., Baskin D., Hood L., Loeb L.A. Random mutagenesis of Thermus aquaticus DNA polymerase I concordance of immutable sites in vivo with the crystal structure. Proc. Natl Acad. Sci. USA. 93:1996;9670-9675
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 9670-9675
    • Suzuki, M.1    Baskin, D.2    Hood, L.3    Loeb, L.A.4
  • 73
    • 0023371227 scopus 로고
    • DNA sequence analysis with a modified bacteriophage T7 DNA polymerase
    • Tabor S., Richardson C.C. DNA sequence analysis with a modified bacteriophage T7 DNA polymerase. Proc. Natl Acad. Sci. USA. 84:1987;4767-4771
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 4767-4771
    • Tabor, S.1    Richardson, C.C.2
  • 74
    • 0006962619 scopus 로고
    • Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I
    • Tabor S., Richardson C.C. Effect of manganese ions on the incorporation of dideoxynucleotides by bacteriophage T7 DNA polymerase and Escherichia coli DNA polymerase I. Proc. Natl Acad. Sci. USA. 86:1989;4076-4080
    • (1989) Proc. Natl Acad. Sci. USA , vol.86 , pp. 4076-4080
    • Tabor, S.1    Richardson, C.C.2
  • 75
    • 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. USA. 92:1995;6339-6343
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6339-6343
    • Tabor, S.1    Richardson, C.C.2
  • 77
    • 0027469780 scopus 로고
    • Cloning of the DNA polymerase gene of Bacillus caldotenax and characterization of the gene product
    • Uemori T., Ishino Y., Fujita K., Asada K., Kato I. Cloning of the DNA polymerase gene of Bacillus caldotenax and characterization of the gene product. J. Biochem. 113:1993;401-410
    • (1993) J. Biochem. , vol.113 , pp. 401-410
    • Uemori, T.1    Ishino, Y.2    Fujita, K.3    Asada, K.4    Kato, I.5
  • 78
    • 0015501746 scopus 로고
    • Studies on polynucleotides. a further study of ribonucleotide incorporation into deoxyribonucleic acid chains by deoxyribonucleic acid polymerase I of Escherichia coli
    • Van de Sande J.H., Loewen P.C., Khorana H.G. Studies on polynucleotides. A further study of ribonucleotide incorporation into deoxyribonucleic acid chains by deoxyribonucleic acid polymerase I of Escherichia coli. J. Biol. Chem. 247:1972;6140-6148
    • (1972) J. Biol. Chem. , vol.247 , pp. 6140-6148
    • Van De Sande, J.H.1    Loewen, P.C.2    Khorana, H.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.