메뉴 건너뛰기




Volumn 16, Issue 9, 2009, Pages 979-986

Structural basis of high-fidelity DNA synthesis by yeast DNA polymerase Δ

Author keywords

[No Author keywords available]

Indexed keywords

DEOXYCYTIDINE TRIPHOSPHATE; DNA DIRECTED DNA POLYMERASE DELTA; EXONUCLEASE; NUCLEOTIDE;

EID: 69949128706     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.1663     Document Type: Article
Times cited : (212)

References (60)
  • 2
    • 38049125552 scopus 로고    scopus 로고
    • The fidelity of DNA synthesis by eukaryotic replicatlve and transleslon synthesis polymerases
    • McCulloch, S.D. & Kunkel, T.A. The fidelity of DNA synthesis by eukaryotic replicatlve and transleslon synthesis polymerases. Cell Res. 18, 148-161 (2008).
    • (2008) Cell Res. , vol.18
    • McCulloch, S.D.1    Kunkel, T.A.2
  • 3
    • 22244478079 scopus 로고    scopus 로고
    • Cellular DNA replicases: Components and dynamics at the replication fork
    • DOI 10.1146/annurev.biochem.73.011303.073859
    • Johnson, A. & O'Donnell, M. Cellular DNA replicases: components and dynamics at the replication fork. Annu. Rev. Biochem. 74, 283-315 (2005). (Pubitemid 40995509)
    • (2005) Annual Review of Biochemistry , vol.74
    • Johnson, A.1    O'Donnell, M.2
  • 4
    • 0024430208 scopus 로고
    • Structure and function of the Saccharomyces cerevisiae CDC2 gene encoding the large subunit of DNA polymerase III
    • Boulet, A., Simon, M., Faye, G., Bauer, G.A. & Burgers, P.M. Structure and function of the Saccharomyces cerevisiae CDC2 gene encoding the large subunit of DNA polymerase III. EMBOJ. 8, 1849-1854 (1989).
    • (1989) EMBOJ , vol.8
    • Boulet, A.1    Simon, M.2    Faye, G.3    Bauer, G.A.4    Burgers, P.M.5
  • 5
    • 0017138261 scopus 로고
    • Sequential function of gene products relative to DNA synthesis in the yeast cell cycle
    • Hartwell, L.H. Sequential function of gene products relative to DNA synthesis in the yeast cell cycle. J. Mol. Biol. 104, 803-817 (1976).
    • (1976) J. Mol. Biol , vol.104
    • Hartwell, L.H.1
  • 6
    • 0025900035 scopus 로고
    • The 3′ to 5′ exonuclease activity located in the DNA polymerase δ subunit of Saccharomyces cerevisiae is required for accurate replication
    • Simon,M.,Glot,L.&Faye,G.The3′- 5′ exonucleaseactivitylocatedintheDNApolymerase 8subunitofSaccharomycescerevisiaeIsrequiredforaccuratereplication.EMBOJ.10, 2165-2170(1991).(Pubitemid21905688)
    • (1991) EMBO Journal , vol.10 , Issue.8
    • Simon, M.1    Giot, L.2    Faye, G.3
  • 7
    • 0024977355 scopus 로고
    • DNA polymerase III, a second essential DNA polymerase, is encoded by the S. cerevisiae CDC2 gene
    • Sitney, K.C., Budd, M.E. & Campbell, J.L. DNA polymerase III, a second essential DNA polymerase, is encoded by the S. cerevisiae CDC2 gene. Cell 56, 599-605 (1989).
    • (1989) Cell , vol.56
    • Sitney, K.C.1    Budd, M.E.2    Campbell, J.L.3
  • 8
    • 0037180555 scopus 로고    scopus 로고
    • High Incidence of epithelial cancers in mice deficient for DNA polymerase 8 proofreading
    • Goldsby, R.E. et al. High Incidence of epithelial cancers In mice deficient for DNA polymerase 8 proofreading. Proc. Natl. Acad. Sci. USA 99, 15560-15565 (2002).
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99
    • Goldsby, R.E.1
  • 9
    • 0034958108 scopus 로고    scopus 로고
    • Defective DNA polymerase-8 proofreading causes cancer susceptibility in mice
    • Goldsby, R.E. et al. Defective DNA polymerase-8 proofreading causes cancer susceptibility In mice. Nat. Med. 7, 638-639 (2001).
    • (2001) Nat. Med , vol.7
    • Goldsby, R.E.1
  • 10
    • 35648999490 scopus 로고    scopus 로고
    • Mutation at the polymerase active site of mouse DNA polymerase 8 increases genomic instability and accelerates tumorigenesls
    • Venkatesan, R.N. et al. Mutation at the polymerase active site of mouse DNA polymerase 8 increases genomic instability and accelerates tumorigenesls. MoI. Cell. Biol. 27, 7669-7682 (2007).
    • (2007) MoI. Cell. Biol , vol.27
    • Venkatesan, R.N.1
  • 11
    • 0033559182 scopus 로고    scopus 로고
    • Detection of mutations in the DNA polymerase δ gene of human sporadic colorectal cancers and colon cancer cell lines
    • DOI 10.1002/(SICI)1097-0215(19990315)80:6<919::AID-IJC19>3.0.CO;2-U
    • Flohr, T. et al. Detection of mutations In the DNA polymerase 8gene of human sporadic colorectal cancers and colon cancer cell lines. Int. J. Cancer 80, 919-929 (1999). (Pubitemid 29108869)
    • (1999) International Journal of Cancer , vol.80 , Issue.6
    • Flohr, T.1    Dai, J.C.2    Buttner, J.3    Popanda, O.4    Hagmuller, E.5    Thielmann, H.W.6
  • 12
    • 0028859670 scopus 로고
    • Polymerase 8 variants in RER colorectal tumours
    • da Costa, L.T. et al. Polymerase 8 variants In RER colorectal tumours. Nat. Genet. 9, 10-11 (1995).
    • (1995) Nat. Genet , vol.9
    • Da Costa, L.T.1
  • 13
    • 0032712407 scopus 로고    scopus 로고
    • A mutation detected in DNA polymerase δ cDNA from Novikoff hepatoma cells correlates with abnormal catalytic properties of the enzyme
    • DOI 10.1007/s004320050322
    • Popanda, O., Flohr, T., Fox, G. & Thielmann, H.W. A mutation detected In DNA polymerase 8 cDNA from Novikoff hepatoma cells correlates with abnormal catalytic properties of the enzyme. J. Cancer Res. Clin. Oncol. 125, 598-608 (1999). (Pubitemid 29502340)
    • (1999) Journal of Cancer Research and Clinical Oncology , vol.125 , Issue.11
    • Popanda, O.1    Flohr, T.2    Fox, G.3    Thielmann, H.W.4
  • 14
    • 34447336941 scopus 로고    scopus 로고
    • Yeast DNA polymerase ε participates in leading-strand DNA replication
    • DOI 10.1126/science.1144067
    • Purseil, Z.F., Isoz, I., Lundstrom, E.B., Johansson, E. & Kunkel, T.A. Yeast DNA polymerase ε participates In leadlng-strand DNA replication. Science 317, 127-130 (2007). (Pubitemid 47056472)
    • (2007) Science , vol.317 , Issue.5834
    • Pursell, Z.F.1    Isoz, I.2    Lundstrom, E.B.3    Johansson, E.4    Kunkel, T.A.5
  • 15
    • 21244506437 scopus 로고    scopus 로고
    • Eukaryotic translesion synthesis DNA polymerases: Specificity of structure and function
    • DOI 10.1146/annurev.biochem.74.082803.133250
    • Prakash, S., Johnson, R.E. & Prakash, L. Eukaryotic transleslon synthesis DNA polymerases: specificity of structure and function. Annu. Rev. Biochem. 74, 317-353 (2005). (Pubitemid 40995510)
    • (2005) Annual Review of Biochemistry , vol.74
    • Prakash, S.1    Johnson, R.E.2    Prakash, L.3
  • 17
    • 0035369086 scopus 로고    scopus 로고
    • Structure of the replicating complex of a pol α family DNA polymerase
    • DOI 10.1016/S0092-8674(01)00367-1
    • Franklin, M.C., Wang, J. & Steltz, T.A. Structure of the replicating complex of a pol a family DNA polymerase. Cell 105, 657-667 (2001). (Pubitemid 32524118)
    • (2001) Cell , vol.105 , Issue.5
    • Franklin, M.C.1    Wang, J.2    Steitz, T.A.3
  • 18
    • 0032518398 scopus 로고    scopus 로고
    • Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution
    • DOI 10.1038/34593
    • Doubllé, 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, 251-258 (1998). (Pubitemid 28099004)
    • (1998) Nature , vol.391 , Issue.6664
    • Doublie, S.1    Tabor, S.2    Long, A.M.3    Richardson, C.C.4    Ellenberger, T.5
  • 19
    • 0032535528 scopus 로고    scopus 로고
    • Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: Structural basis for nucleotide incorporation
    • DOI 10.1093/emboj/17.24.7514
    • Li, Y., Korolev, S. & Waksman, G. Crystal structures of open and closed forms of binary and ternary complexes of the large fragment of Thermus aquaticus DNA polymerase I: structural basis for nucleotide Incorporation. EMBO J. 17, 7514-7525 (1998). (Pubitemid 29002718)
    • (1998) EMBO Journal , vol.17 , Issue.24
    • Li, Y.1    Korolev, S.2    Waksman, G.3
  • 20
    • 1642588255 scopus 로고    scopus 로고
    • Structures of mismatch replication errors observed in a DNA polymerase
    • Johnson, S.J. & Beese, L.S. Structures of mismatch replication errors observed In a DNA polymerase. Cell 116, 803-816 (2004).
    • (2004) Cell , vol.116
    • Johnson, S.J.1    Beese, L.S.2
  • 22
    • 33847706180 scopus 로고    scopus 로고
    • Structural and biochemical investigation of the role in proofreading of a β hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B family
    • DOI 10.1074/jbc.M605675200
    • Hogg, M., Aller, P., Koigsberg, W., Wallace, S.S. & Doublie, S. Structural and biochemical Investigation of the role In proofreading of a ß hairpin loop found in the exonuclease domain of a replicative DNA polymerase of the B family. J. Biol. Chem. 282, 1432-1444 (2007). (Pubitemid 47076520)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.2
    • Hogg, M.1    Aller, P.2    Konigsberg, W.3    Wallace, S.S.4    Doublie, S.5
  • 23
    • 0032483409 scopus 로고    scopus 로고
    • The proofreading pathway of bacteriophage T4 DNA polymerase
    • Reha-Krantz, L.J. et al. The proofreading pathway of bacteriophage T4 DNA polymerase. J. Biol. Chem. 273, 22969-22976 (1998).
    • (1998) J. Biol. Chem , vol.273
    • Reha-Krantz, L.J.1
  • 24
    • 0028892405 scopus 로고
    • Dynamics of bacteriophage T4 DNA polymerase function: Identification of amino acid residues that affect switching between polymerase and 3′ -> 5′ exonuclease activities
    • Stockl, S.A., Nonay, R.L. & Reha-Krantz, L.J. Dynamics of bacteriophage T4 DNA polymerase function: identification of amino acid residues that affect switching between polymerase and 3′ -> 5′ exonuclease activities. J. Mol. Biol. 254, 15-28 (1995).
    • (1995) J. Mol. Biol , vol.254
    • Stockl, S.A.1    Nonay, R.L.2    Reha-Krantz, L.J.3
  • 25
    • 0024464048 scopus 로고
    • Locations of amino acid substitutions in bacteriophage T4 tsL56 DNA polymerase predict an N-termlnal exonuclease domain
    • Reha-Krantz, L.J. Locations of amino acid substitutions In bacteriophage T4 tsL56 DNA polymerase predict an N-termlnal exonuclease domain. J. Virol. 63, 4762-4766 (1989).
    • (1989) J. Virol , vol.63
    • Reha-Krantz, L.J.1
  • 26
    • 0032552971 scopus 로고    scopus 로고
    • Kinetic characterization of a bacteriophage T4 antimutator DNA polymerase
    • DOI 10.1021/bi980835a
    • Wu, P., Nossal, N. & Benkovic, S.J. Kinetic characterization of a bacteriophage T4 antimutator DNA polymerase. Biochemistry 37, 14748-14755 (1998). (Pubitemid 28487582)
    • (1998) Biochemistry , vol.37 , Issue.42
    • Wu, P.1    Nossal, N.2    Benkovic, S.J.3
  • 27
    • 25844440534 scopus 로고    scopus 로고
    • Biochemistry: Rev1 employs a novel mechanism of DNA synthesis using a protein template
    • DOI 10.1126/science.1116336
    • Nair, D.T., Johnson, R.E., Prakash, L., Prakash, S. & Aggarwal, A.K. Revi employs a novel mechanism of DNA synthesis using a protein template. Science 309, 2219-2222 (2005). (Pubitemid 41396072)
    • (2005) Science , vol.309 , Issue.5744
    • Nair, D.T.1    Johnson, R.E.2    Prakash, L.3    Prakash, S.4    Aggarwal, A.K.5
  • 28
    • 0032582787 scopus 로고    scopus 로고
    • Role of the first aspartate residue of the "YxDTDS" motif of Φ29 DNA polymerase as a metal ligand during both TP-primed and DNA-primed DNA synthesis
    • Saturno, J., Lazaro, J.M., Blanco, L. & Salas, M. Role of the first aspartate residue of the "YxDTDS" motif of Φ29 DNA polymerase as a metal ligand during both TP-primed and DNA-primed DNA synthesis. J. Mol. Biol. 283, 633-642 (1998).
    • (1998) J. Mol. Biol , vol.283
    • Saturno, J.1    Lazaro, J.M.2    Blanco, L.3    Salas, M.4
  • 30
    • 0027233686 scopus 로고
    • Mutational analysis of the human DNA polymerasea. the most conserved region in α-like DNA polymerases Is involved in metal-specific catalysis
    • 31.
    • Copeland, W.C. & Wang, T.S. Mutational analysis of the human DNA polymerasea. The most conserved region In α-like DNA polymerases Is involved in metal-specific catalysis. J. Biol. Chem. 268, 11028-11040 (1993). 31.
    • (1993) J. Biol. Chem , vol.268
    • Copeland, W.C.1    Wang, T.S.2
  • 31
    • 33947381026 scopus 로고    scopus 로고
    • The roles of Tyr391 and Tyr619 in RB69 DNA polymerase replication fidelity
    • Jacewlcz, A., Makiela, K., Kierzek, A., Drake, J.W. & Bebenek, A. The roles of Tyr391 and Tyr619 in RB69 DNA polymerase replication fidelity. J. Mol. Biol. 368, 18-29 (2007).
    • (2007) J. Mol. Biol , vol.368
    • Jacewlcz, A.1    Makiela, K.2    Kierzek, A.3    Drake, J.W.4    Bebenek, A.5
  • 32
    • 14644432415 scopus 로고    scopus 로고
    • Base selectivity is impaired by mutants that perturb hydrogen bonding networks in the RB69 DNA polymerase active site
    • DOI 10.1021/bi047921x
    • Yang, G., Wang, J. & Königsberg, W. Base selectivity Is impaired by mutants that perturb hydrogen bonding networks In the RB69 DNA polymerase active site. Biochemistry 44, 3338-3346 (2005). (Pubitemid 40322004)
    • (2005) Biochemistry , vol.44 , Issue.9
    • Yang, G.1    Wang, J.2    Konigsberg, W.3
  • 33
    • 2342537864 scopus 로고    scopus 로고
    • Crystallographic snapshots of a replicative DNA polymerase encountering an abasic site
    • DOI 10.1038/sj.emboj.7600150
    • Hogg, M., Wallace, S.S. & Doublie, S. Crystallography snapshots of a replicatlve DNA polymerase encountering an abasic site. EMBO J. 23, 1483-1493 (2004). (Pubitemid 38579509)
    • (2004) EMBO Journal , vol.23 , Issue.7
    • Hogg, M.1    Wallace, S.S.2    Doublie, S.3
  • 34
    • 33645216188 scopus 로고    scopus 로고
    • Mutator phenotypes caused by substitution at a conserved motif A residue in eukaryotic DNA polymerase 8
    • Venkatesan, R.N., Hsu, J.J., Lawrence, N.A., Preston, B.D. & Loeb, L.A. Mutator phenotypes caused by substitution at a conserved motif A residue in eukaryotic DNA polymerase 8. J. Biol. Chem. 281, 4486-4494 (2006).
    • (2006) J. Biol. Chem , vol.281
    • Venkatesan, R.N.1    Hsu, J.J.2    Lawrence, N.A.3    Preston, B.D.4    Loeb, L.A.5
  • 36
    • 0037176870 scopus 로고    scopus 로고
    • Correlation of the kinetics of finger domain mutants in RB69 DNA polymerase with its structure
    • DOI 10.1021/bi0119924
    • Yang, G., Franklin, M., Li, J., Lin, T.C. & Konigsberg, W. Correlation of the kinetics of finger domain mutants In RB69 DNA polymerase with its structure. Biochemistry 41, 2526-2534 (2002). (Pubitemid 34168921)
    • (2002) Biochemistry , vol.41 , Issue.8
    • Yang, G.1    Franklin, M.2    Li, J.3    Lin, T.C.4    Konigsberg, W.5
  • 37
    • 0037072265 scopus 로고    scopus 로고
    • A conserved Tyr residue is required for sugar selectivity in a pol α DNA polymerase
    • DOI 10.1021/bi0202171
    • Yang, G., Franklin, M., Li, J., Lin, T.C. & Konigsberg, W. A conserved Tyr residue Is required for sugar selectivity in a Pol a DNA polymerase. Biochemistry 41, 10256-10261 (2002). (Pubitemid 34856450)
    • (2002) Biochemistry , vol.41 , Issue.32
    • Yang, G.1    Franklin, M.2    Li, J.3    Lin, T.C.4    Konigsberg, W.5
  • 38
    • 0033594982 scopus 로고    scopus 로고
    • Steady-state kinetic characterization of RB69 DNA polymerase mutants that affect dNTP incorporation
    • Yang G., Lin T.C., Karam J., Konigsberg W.H. Steady-state kinetic characterization of RB69 DNA polymerase mutants that affect dNTP incorporation. Biochemistry, 1999.
    • (1999) Biochemistry , vol.38 , Issue.25
    • Yang, G.1    Lin, T.C.2    Karam, J.3    Konigsberg, W.H.4
  • 40
    • 0022505062 scopus 로고
    • Structure of an adenine-cytosine base pair in DNA and its implications for mismatch repair
    • Hunter W.N., Brown T., Anand N.N., Kennard O. Structure of an adenine-cytosine base pair in DNA and its implications for mismatch repair. Nature (1996) 320, 6062.
    • (1986) Nature , vol.320 , Issue.6062
    • Hunter, W.N.1    Brown, T.2    Anand, N.N.3    Kennard, O.4
  • 41
    • 0023664744 scopus 로고
    • The structure of guanosine-thymidlne mismatches in B-DNA at 2.5-Å resolution
    • Hunter, W.N. et al. The structure of guanosine-thymidlne mismatches In B-DNA at 2.5-Å resolution. J. Biol. Chem. 262, 9962-9970 (1987).
    • (1987) J. Biol. Chem , vol.262
    • Hunter, W.N.1
  • 42
    • 0027247430 scopus 로고
    • Oligonucleotide x-ray structures in the study of conformation and interactions of nucleic acids
    • Kennard,O.&Salisbury,S.A.OligonucleotideX- raystructuresInthestudyofconformationandInteractionsofnucleicacids.J.Biol.Chem. 268,10701-10704(1993).(Pubitemid23162241)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.15
    • Kennard, O.1    Salisbury, S.A.2
  • 43
    • 0037102491 scopus 로고    scopus 로고
    • The non-Watson-Crick base pairs and their associated isostericity matrices
    • Leontis N.B., Stombaugh J., Westhof E., The non-Watson-Crick base pairs and their associated isostericity matrices. Nucleic Acids Research (2002) 30, 16.
    • (2002) Nucleic Acids Research , vol.30 , Issue.16
    • Leontis, N.B.1    Stombaugh, J.2    Westhof, E.3
  • 44
    • 0023628497 scopus 로고
    • Helix geometry, hydration, and G.A mismatch in a B-DNA decamer
    • Privé, G.G. et al. Helix geometry, hydration, and G.A mismatch In a B-DNA decamer. Science 238, 498-504 (1987).
    • (1987) Science , vol.238
    • Privé, G.G.1
  • 45
    • 23844522523 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae DNA polymerase 8: High fidelity for base substitutions but lower fidelity for single- And multi-base deletions
    • Fortune, J.M. et al. Saccharomyces cerevisiae DNA polymerase 8: high fidelity for base substitutions but lower fidelity for single- and multi-base deletions. J. Biol. Chem. 280, 29980-29987 (2005).
    • (2005) J. Biol. Chem , vol.280
    • Fortune, J.M.1
  • 46
    • 0026464542 scopus 로고
    • Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4
    • Capson, T.L. et al. Kinetic characterization of the polymerase and exonuclease activities of the gene 43 protein of bacteriophage T4. Biochemistry 31, 10984-10994 (1992).
    • (1992) Biochemistry , vol.31
    • Capson, T.L.1
  • 47
    • 0025963376 scopus 로고
    • Kinetic partitioning between the exonuclease and polymerase sites in DNA error correction
    • Donlln, M.J., Patel, S.S. & Johnson, K.A. Kinetic partitioning between the exonuclease and polymerase sites In DNA error correction. Biochemistry 30, 538-546 (1991).
    • (1991) Biochemistry , vol.30
    • Donlln, M.J.1    Patel, S.S.2    Johnson, K.A.3
  • 48
    • 58549083754 scopus 로고    scopus 로고
    • Structure of PoIC reveals unique DNA binding and fidelity determinants
    • Evans, R.J. et al. Structure of PoIC reveals unique DNA binding and fidelity determinants. Proc. Natl. Acad. Sci. USA 105, 20695-20700 (2008).
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105
    • Evans, R.J.1
  • 49
    • 0028085880 scopus 로고
    • Isolation, characterization kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3′-5′ exonuclease activity
    • Lin T.C., Karam G., Konigsberg W.H. Isolation, characterization kinetic properties of truncated forms of T4 DNA polymerase that exhibit 3′-5′ exonuclease activity. Journal of Biological Chemistry (1994) 269, 30.
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.30
    • Lin, T.C.1    Karam, G.2    Konigsberg, W.H.3
  • 50
    • 0026643492 scopus 로고
    • Processive proofreading is Intrinsic to T4 DNA polymerase
    • Reddy, M.K., Weitzel, S.E. & von Hippel, P.H. Processive proofreading is Intrinsic to T4 DNA polymerase. J. Biol. Chem. 267, 14157-14166 (1992).
    • (1992) J. Biol. Chem. , vol.267
    • Reddy, M.K.1    Weitzel, S.E.2    Von Hippel, P.H.3
  • 51
    • 0024395470 scopus 로고
    • How DNA travels between the separate polymerase and 3′-5′- exonuclease sites of DNA polymerase i (Klenow fragment)
    • Joyce, C.M. How DNA travels between the separate polymerase and 3′-5′-exonuclease sites of DNA polymerase I (Klenow fragment). J. Biol. Chem. 264, 10858-10866 (1989).
    • (1989) J. Biol. Chem. , vol.264
    • Joyce, C.M.1
  • 52
    • 0031030449 scopus 로고    scopus 로고
    • Structure of the single-stranded-DNA-binding domain of replication protein A bound to DNA
    • DOI 10.1038/385176a0
    • Bochkarev, A., Pfuetzner, R.A., Edwards, A.M. & Frappier, L. Structure of the slngle-stranded-DNA-blnding domain of replication protein A bound to DNA. Nature 385, 176-181 (1997). (Pubitemid 27034221)
    • (1997) Nature , vol.385 , Issue.6612
    • Bochkarev, A.1    Pfuetzner, R.A.2    Edwards, A.M.3    Frappier, L.4
  • 53
    • 0031047632 scopus 로고    scopus 로고
    • Crystal structure of the two RNA binding domains of human hnRNP A1 at 1.75 A resolution
    • DOI 10.1038/nsb0397-215
    • Shamoo, Y., Krueger, U., Rice, L.M., Williams, K.R. & Steitz, T.A. Crystal structure of the two RNA binding domains of human hnRNP Al at 1.75 Â resolution. Nat. Struct. Biol. A, 215-222 (1997). (Pubitemid 27111168)
    • (1997) Nature Structural Biology , vol.4 , Issue.3
    • Shamoo, Y.1    Krueger, U.2    Rice, L.M.3    Williams, K.R.4    Steitz, T.A.5
  • 54
    • 63249130106 scopus 로고    scopus 로고
    • Polymerase dynamics at the eukaryotic DNA replication fork
    • Burgers, P.M. Polymerase dynamics at the eukaryotic DNA replication fork. J. Biol. Chem. 284, 4041-4045 (2009).
    • (2009) J. Biol. Chem , vol.284
    • Burgers, P.M.1
  • 55
    • 57649129186 scopus 로고    scopus 로고
    • The replisome uses mRNA as a primer after colliding with RNA polymerase
    • Pomerantz, R.T. & O'Donnell, M. The replisome uses mRNA as a primer after colliding with RNA polymerase. Nature 456, 762-766 (2008).
    • (2008) Nature , vol.456
    • Pomerantz, R.T.1    O'Donnell, M.2
  • 56
    • 33745219847 scopus 로고    scopus 로고
    • Yeast and Human Translesion DNA Synthesis Polymerases: Expression, Purification, and Biochemical Characterization
    • DOI 10.1016/S0076-6879(06)08024-4, PII S0076687906080244
    • Johnson, R.E., Prakash, L. & Prakash, S. Yeast and human translesion DNA synthesis polymerases: expression, purification, and biochemical characterization. Methods Enzymol. 408, 390-407 (2006). (Pubitemid 43912267)
    • (2006) Methods in Enzymology , vol.408
    • Johnson, R.E.1    Prakash, L.2    Prakash, S.3
  • 57
    • 0031058188 scopus 로고    scopus 로고
    • Maximum-likelihood heavy-atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods
    • DOI 10.1016/S0076-6879(97)76073-7
    • 57.de La Fortelle, E. & Bricogne, G. Maximum-likelihood heavy atom parameter refinement for multiple isomorphous replacement and multiwavelength anomalous diffraction methods. Methods Enzymol. 276, 472-494 (1997). (Pubitemid 27085618)
    • (1997) Methods in Enzymology , vol.276
    • De La Fortelle, E.1    Bricogne, G.2
  • 58
    • 0030038464 scopus 로고    scopus 로고
    • Methods used in the structure determination of bovine mitochondrial Fl ATPase
    • Abrahams, J.P. & Leslie, A.G. Methods used In the structure determination of bovine mitochondrial Fl ATPase. Acta Crystallogr. D Biol. Crystallogr. 52, 30-42 (1996).
    • (1996) Acta Crystallogr. D Biol. Crystallogr , vol.52
    • Abrahams, J.P.1    Leslie, A.G.2
  • 60
    • 0013461295 scopus 로고    scopus 로고
    • Macromolecular TLS refinement in REFMAC at moderate resolutions
    • Winn, M.D., Murshudov, G.N. & Paplz, M.Z. Macromolecular TLS refinement in REFMAC at moderate resolutions. Methods Enzymol. 374, 300-321 (2003).
    • (2003) Methods Enzymol. , vol.374
    • Winn, M.D.1    Murshudov, G.N.2    Paplz, M.Z.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.