메뉴 건너뛰기




Volumn 188, Issue 12, 2006, Pages 4464-4473

Structure of the θ subunit of Escherichia coli DNA polymerase III in complex with the ε subunit

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL ENZYME; BUFFER; DNA DIRECTED DNA POLYMERASE GAMMA; DNA POLYMERASE III ALPHA; DNA POLYMERASE III EPSILON; DNA POLYMERASE III THETA; DYSPROSIUM; EPITOPE; ERBIUM; HOLMIUM; LANTHANIDE; METHANOL; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 33744968001     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.01992-05     Document Type: Article
Times cited : (24)

References (56)
  • 1
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., T.-H. Xia, M. Billeter, P. Güntert, and K. Wüthrich. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 6:1-10.
    • (1995) J. Biomol. NMR , vol.6 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 3
    • 23644435321 scopus 로고    scopus 로고
    • Bacteriophage P1 hot gene product can substitute for the E. coli DNA polymerase III θ subunit
    • Chikova, A. K., and R. M. Schaaper. 2005. Bacteriophage P1 hot gene product can substitute for the E. coli DNA polymerase III θ subunit. J. Bacteriol. 187:5528-5536.
    • (2005) J. Bacteriol. , vol.187 , pp. 5528-5536
    • Chikova, A.K.1    Schaaper, R.M.2
  • 4
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • Cornilescu, G., F. Delaglio, and A. Bax. 1999. Protein backbone angle restraints from searching a database for chemical shift and sequence homology. J. Biomol. NMR 13:289-302.
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 6
    • 0037426325 scopus 로고    scopus 로고
    • Elucidation of the ε-θ interface of Escherichia coli DNA polymerase III by NMR spectroscopy
    • DeRose, E. F., T. Darden, S. Harvey, S., Gabel, F. W. Perrino, R. M. Schaaper, and R. E. London. 2003. Elucidation of the ε-θ interface of Escherichia coli DNA polymerase III by NMR spectroscopy. Biochemistry 42:3635-3644.
    • (2003) Biochemistry , vol.42 , pp. 3635-3644
    • DeRose, E.F.1    Darden, T.2    Harvey, S.3    Gabel, S.4    Perrino, F.W.5    Schaaper, R.M.6    London, R.E.7
  • 7
    • 9944257036 scopus 로고    scopus 로고
    • Phage like it HOT: Solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the θ subunit of E. coli DNA polymerase III
    • DeRose, E. F., T. W. Kirby, G. A. Mueller, A. K. Chikova, R. M. Schaaper, and R. E. London. 2004. Phage like it HOT: solution structure of the bacteriophage P1-encoded HOT protein, a homolog of the θ subunit of E. coli DNA polymerase III. Structure 12:2221-2231.
    • (2004) Structure , vol.12 , pp. 2221-2231
    • DeRose, E.F.1    Kirby, T.W.2    Mueller, G.A.3    Chikova, A.K.4    Schaaper, R.M.5    London, R.E.6
  • 8
    • 0037039423 scopus 로고    scopus 로고
    • Model for the catalytic domain of the proofreading ε subunit of Escherichia coli DNA polymerase III based on NMR structural data
    • DeRose, E. F., D. W. Li, T. Darden, S. Harvey, F. W. Perrino, R. M. Schaaper, and R. E. London. 2002. Model for the catalytic domain of the proofreading ε subunit of Escherichia coli DNA polymerase III based on NMR structural data. Biochemistry 41:94-110.
    • (2002) Biochemistry , vol.41 , pp. 94-110
    • DeRose, E.F.1    Li, D.W.2    Darden, T.3    Harvey, S.4    Perrino, F.W.5    Schaaper, R.M.6    London, R.E.7
  • 9
    • 0029929070 scopus 로고    scopus 로고
    • The helix-hairpin-helix DNA-binding motif: A structural basis for non-sequence-specific recognition of DNA
    • Doherty, A. J., L. C. Serpell, and C. P. Ponting. 1996. The helix-hairpin-helix DNA-binding motif: a structural basis for non-sequence-specific recognition of DNA. Nucleic Acids Res. 24:2488-2497.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 2488-2497
    • Doherty, A.J.1    Serpell, L.C.2    Ponting, C.P.3
  • 10
    • 0034891022 scopus 로고    scopus 로고
    • Mapping the ligand binding site at protein side-chains in protein-ligand complexes through NOE difference spectroscopy
    • Eichmüller, C., M. Tollinger, B. Kräutler, and R. Konrat. 2001. Mapping the ligand binding site at protein side-chains in protein-ligand complexes through NOE difference spectroscopy. J. Biomol. NMR 20:195-202.
    • (2001) J. Biomol. NMR , vol.20 , pp. 195-202
    • Eichmüller, C.1    Tollinger, M.2    Kräutler, B.3    Konrat, R.4
  • 11
    • 58149362646 scopus 로고
    • Sequential protein backbone resonance assignments using an improved 3D-HN(CA)CO pulse scheme
    • Engelke, J., and H. Rüterjans. 1995. Sequential protein backbone resonance assignments using an improved 3D-HN(CA)CO pulse scheme. J. Magn. Reson. B 109:318-322.
    • (1995) J. Magn. Reson. B , vol.109 , pp. 318-322
    • Engelke, J.1    Rüterjans, H.2
  • 12
    • 0004757060 scopus 로고    scopus 로고
    • University of California, San Francisco
    • Goddard, T. D., and D. G. Kneller. 2003. Sparky, University of California, San Francisco.
    • (2003) Sparky
    • Goddard, T.D.1    Kneller, D.G.2
  • 14
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek, S., and A. Bax. 1992. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J. Am. Chcm. Soc. 114:6291-6293.
    • (1992) J. Am. Chcm. Soc. , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 16
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., C. Mumenthaler, and K. Wüthrich. 1997. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J. Mol. Biol. 273:283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 17
    • 7244239509 scopus 로고    scopus 로고
    • Application of electrospray ionization mass spectrometry to study the hydrophohic interaction between then ε and θ subunits of DNA polymerase III
    • Gupta, R., S. M. Hamdan, N. E. Dixon, M. M. Sheil, and J. L. Beck. 2004. Application of electrospray ionization mass spectrometry to study the hydrophohic interaction between then ε and θ subunits of DNA polymerase III. Protein Sci. 13:2878-2887.
    • (2004) Protein Sci. , vol.13 , pp. 2878-2887
    • Gupta, R.1    Hamdan, S.M.2    Dixon, N.E.3    Sheil, M.M.4    Beck, J.L.5
  • 18
    • 0033792973 scopus 로고    scopus 로고
    • Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the ε subunit of Escherichia coli DNA polymerase III
    • Hamdan, S., S. E. Brown, P. R. Thompson, J. Y. Yang, P. D. Carr, D. L. Ollis, G. Otting, and N. E. Dixon. 2000. Preliminary X-ray crystallographic and NMR studies on the exonuclease domain of the ε subunit of Escherichia coli DNA polymerase III. J. Struct. Biol. 131:164-169.
    • (2000) J. Struct. Biol. , vol.131 , pp. 164-169
    • Hamdan, S.1    Brown, S.E.2    Thompson, P.R.3    Yang, J.Y.4    Carr, P.D.5    Ollis, D.L.6    Otting, G.7    Dixon, N.E.8
  • 20
    • 0036229246 scopus 로고    scopus 로고
    • Structural basis for proofreading during replication of the Escherichia coli chromosome
    • Hamdan, S., P. D. Carr, S. E. Brown, D. L. Ollis, and N. E. Dixon. 2002. Structural basis for proofreading during replication of the Escherichia coli chromosome. Structure 10:535-546.
    • (2002) Structure , vol.10 , pp. 535-546
    • Hamdan, S.1    Carr, P.D.2    Brown, S.E.3    Ollis, D.L.4    Dixon, N.E.5
  • 21
    • 0025995844 scopus 로고
    • A structure taxonomy of DNA-binding domains
    • Harrison, S. C. 1991. A structure taxonomy of DNA-binding domains. Nature 353:715-719.
    • (1991) Nature , vol.353 , pp. 715-719
    • Harrison, S.C.1
  • 22
    • 0036308102 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA
    • Herrmann, T., P. Güntert, and K. Wüthrich. 2002. Protein NMR structure determination with automated NOE assignment using the new software CANDID and the torsion angle dynamics algorithm DYANA. J. Mol. Biol. 319:209-227.
    • (2002) J. Mol. Biol. , vol.319 , pp. 209-227
    • Herrmann, T.1    Güntert, P.2    Wüthrich, K.3
  • 23
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and C. Sander. 1993. Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233:123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 24
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure-pattern recognition of hydrogen-bonded and geometrical features
    • Kabsch, W., and C. Sander. 1983. Dictionary of protein secondary structure-pattern recognition of hydrogen-bonded and geometrical features. Biopolymers 22:2577-2637.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 26
    • 0034056323 scopus 로고    scopus 로고
    • NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli
    • Keniry, M. A., H. A. Berthon, J. Y. Yang, C. S. Miles, and N. E. Dixon. 2000. NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli. Protein Sci. 9:721-733.
    • (2000) Protein Sci. , vol.9 , pp. 721-733
    • Keniry, M.A.1    Berthon, H.A.2    Yang, J.Y.3    Miles, C.S.4    Dixon, N.E.5
  • 27
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., M. Billeter, and K. Wüthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics. 14:51-55.
    • (1996) J. Mol. Graphics. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 28
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., J. A. C. Rullmann, M. W. MacArthur, R. Kaptein, and J. M. Thornton. 1996. AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8:477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 30
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structures of protein-protein recognition sites
    • Lo Conte, L., C. Chothia, and J. Janin. 1999. The atomic structures of protein-protein recognition sites. J. Mol. Biol. 285:2177-2198.
    • (1999) J. Mol. Biol. , vol.285 , pp. 2177-2198
    • Lo Conte, L.1    Chothia, C.2    Janin, J.3
  • 32
    • 0034635344 scopus 로고    scopus 로고
    • Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase. Correlation with DNA binding and dRP lyase activity
    • Maciejewski, M. W., D. Liu, R. Prasad, S. H. Wilson, and G. P. Mullen. 2000. Backbone dynamics and refined solution structure of the N-terminal domain of DNA polymerase. Correlation with DNA binding and dRP lyase activity. J. Mol. Biol. 296:229-253.
    • (2000) J. Mol. Biol. , vol.296 , pp. 229-253
    • Maciejewski, M.W.1    Liu, D.2    Prasad, R.3    Wilson, S.H.4    Mullen, G.P.5
  • 33
    • 0022344806 scopus 로고
    • The polymerase subunit of DNA polymerase III of Escherichia coli. I. Amplification of the dnaE gene product and polymerase activity of the α subunit
    • Maki, H., T. Horiuchi, and A. Kornberg. 1985. The polymerase subunit of DNA polymerase III of Escherichia coli. I. Amplification of the dnaE gene product and polymerase activity of the α subunit. J. Biol. Chem. 260:12982-12986.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12982-12986
    • Maki, H.1    Horiuchi, T.2    Kornberg, A.3
  • 34
    • 0022345854 scopus 로고
    • The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the α subunit, devoid of nuclcase activities
    • Maki, H., and A. Kornberg. 1985. The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the α subunit, devoid of nuclcase activities. J. Biol. Chem. 260:12987-12992.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12987-12992
    • Maki, H.1    Kornberg, A.2
  • 35
    • 0023369230 scopus 로고
    • Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunits
    • Maki, H., and A. Kornberg. 1987. Proofreading by DNA polymerase III of Escherichia coli depends on cooperative interaction of the polymerase and exonuclease subunits. Proc. Natl. Acad. Sci. USA 84:4389-4392.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 4389-4392
    • Maki, H.1    Kornberg, A.2
  • 37
    • 0141677891 scopus 로고    scopus 로고
    • Chromosomal replicases as asymmetric dimers: Studies of subunit arrangement and functional consequences
    • McHenry, C. S. 2003. Chromosomal replicases as asymmetric dimers: studies of subunit arrangement and functional consequences. Mol. Microbiol. 49:1157-1165.
    • (2003) Mol. Microbiol. , vol.49 , pp. 1157-1165
    • McHenry, C.S.1
  • 38
    • 0018786252 scopus 로고
    • DNA polymerase III of Escherichia coli. Purification and identification of subunits
    • McHenry, C. S., and W. Crow. 1979. DNA polymerase III of Escherichia coli. Purification and identification of subunits. J. Biol. Chem. 254:1748-1753.
    • (1979) J. Biol. Chem. , vol.254 , pp. 1748-1753
    • McHenry, C.S.1    Crow, W.2
  • 39
    • 26444476481 scopus 로고    scopus 로고
    • Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III θ subunit
    • Mueller, G. A., T. W. Kirby, E. F. DeRose, D. Li, R. M. Schaaper, and R. E. London. 2005. Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III θ subunit. J. Bacteriol. 187:7081-7089.
    • (2005) J. Bacteriol. , vol.187 , pp. 7081-7089
    • Mueller, G.A.1    Kirby, T.W.2    DeRose, E.F.3    Li, D.4    Schaaper, R.M.5    London, R.E.6
  • 41
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram, D. R., and L. E. Kay. 1994. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J. Magn. Reson. B 103:203-216.
    • (1994) J. Magn. Reson. B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 43
    • 0025252231 scopus 로고
    • 1H]-NMR spectroscopy: Combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions
    • 1H]-NMR spectroscopy: combined use with isotope labeling for studies of macromolecular conformation and intermolecular interactions. Q. Rev. Biophys. 23:39-96.
    • (1990) Q. Rev. Biophys. , vol.23 , pp. 39-96
    • Otting, G.1    Wüthrich, K.2
  • 44
    • 0033619538 scopus 로고    scopus 로고
    • Two functional domains of the ε subunit of DNA polymerase III
    • Perrino, F. W., S. Harvey, and S. M. McNeill. 1999. Two functional domains of the ε subunit of DNA polymerase III. Biochemistry 38:16001-16009.
    • (1999) Biochemistry , vol.38 , pp. 16001-16009
    • Perrino, F.W.1    Harvey, S.2    McNeill, S.M.3
  • 46
    • 33645390370 scopus 로고    scopus 로고
    • Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes
    • Pintacuda, G., A. Y. Park, M. A. Keniry, N. E. Dixon, and G. Otting. 2006. Lanthanide labeling offers fast NMR approach to 3D structure determinations of protein-protein complexes. J. Am. Chem. Soc. 128:3696-3702.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 3696-3702
    • Pintacuda, G.1    Park, A.Y.2    Keniry, M.A.3    Dixon, N.E.4    Otting, G.5
  • 47
    • 0024290472 scopus 로고
    • Amino acid preferences for specific locations at the ends of α helices
    • Richardson, J. S., and D. C. Richardson. 1988. Amino acid preferences for specific locations at the ends of α helices. Science 240:1648-1652.
    • (1988) Science , vol.240 , pp. 1648-1652
    • Richardson, J.S.1    Richardson, D.C.2
  • 48
    • 0020981110 scopus 로고
    • Identification of the ε-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: A fidelity subunit for DNA replication
    • Scheuermann, R. H., S. Tam, P. M. J. Burgers, and H. Echols. 1983. Identification of the ε-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: a fidelity subunit for DNA replication. Proc. Natl. Acad. Sci. USA 80:7085-7089.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 7085-7089
    • Scheuermann, R.H.1    Tam, S.2    Burgers, P.M.J.3    Echols, H.4
  • 50
    • 0025122284 scopus 로고
    • Processive replication is contingent on the exonuclease subunil of DNA polymerase III holoenzyme
    • Studwell, P. S., and M. O'Donnell. 1990. Processive replication is contingent on the exonuclease subunil of DNA polymerase III holoenzyme. J. Biol. Chem. 265:1171-1178.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1171-1178
    • Studwell, P.S.1    O'Donnell, M.2
  • 51
    • 0027158172 scopus 로고
    • DNA polymerase III accessory proteins. V. θ encoded by holE
    • Studwell-Vaughan, P. S., and M. O'Donnell. 1993. DNA polymerase III accessory proteins. V. θ encoded by holE J. Biol. Chem. 268:11785-11791.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11785-11791
    • Studwell-Vaughan, P.S.1    O'Donnell, M.2
  • 52
    • 1942539340 scopus 로고    scopus 로고
    • The θ subunit of Escherichia coli DNA polymerase III: A role in stabilizing the ε proofreading subunit
    • Taft-Benz, S. A., and R. M. Schaaper. 2004. The θ subunit of Escherichia coli DNA polymerase III: a role in stabilizing the ε proofreading subunit. J. Bacteriol. 186:2774-2780.
    • (2004) J. Bacteriol. , vol.186 , pp. 2774-2780
    • Taft-Benz, S.A.1    Schaaper, R.M.2
  • 54
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart, D. S., and B. D. Sykes. 1994. Chemical shifts as a tool for structure determination. Methods Enzymol. 239:363-392.
    • (1994) Methods Enzymol. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 56
    • 0028541866 scopus 로고
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques
    • 15N resonance assignments of the N-terminal SH3 domain of drk in folded and unfolded states using enhanced-sensitivity pulsed field gradient NMR techniques. J. Biomol. NMR 4:845-858.
    • (1994) J. Biomol. NMR , vol.4 , pp. 845-858
    • Zhang, O.1    Kay, L.E.2    Olivier, J.P.3    Forman-Kay, J.D.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.