메뉴 건너뛰기




Volumn 9, Issue 4, 2000, Pages 721-733

NMR solution structure of the θ subunit of DNA polymerase III from Escherichia coli

Author keywords

Backbone assignment; Circular dichroism; DNA polymerase; Protein structure; Triple resonance NMR

Indexed keywords

BACTERIAL ENZYME; DNA DIRECTED DNA POLYMERASE GAMMA;

EID: 0034056323     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.9.4.721     Document Type: Article
Times cited : (21)

References (42)
  • 1
    • 0026748968 scopus 로고
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible
    • 15N relaxation using inverse detected two-dimensional NMR spectroscopy: The central helix is flexible. Biochemistry 31:5269-5278.
    • (1992) Biochemistry , vol.31 , pp. 5269-5278
    • Barbato, G.1    Ikura, M.2    Kay, L.E.3    Pastor, R.W.4    Bax, A.5
  • 2
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels C, Xia T-H, Billeter M, Güntert P, Wüthrich K. 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
    • 0028113437 scopus 로고
    • Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy
    • Damberger FF, Pelton JG, Harrison CJ, Nelson HCM, Wemmer DE. 1994. Solution structure of the DNA-binding domain of the heat shock transcription factor determined by multidimensional heteronuclear magnetic resonance spectroscopy. J Biomol NMR 3:1806-1821.
    • (1994) J Biomol NMR , vol.3 , pp. 1806-1821
    • Damberger, F.F.1    Pelton, J.G.2    Harrison, C.J.3    Nelson, H.C.M.4    Wemmer, D.E.5
  • 4
    • 58149362646 scopus 로고
    • Sequential protein backbone resonance assignments using an improved 3D-HN(CA)CO pulse scheme
    • Engelke J, Rüterjans H. 1995. Sequential protein backbone resonance assignments using an improved 3D-HN(CA)CO pulse scheme. J Magn Reson Ser B 109:318-322.
    • (1995) J Magn Reson Ser B , vol.109 , pp. 318-322
    • Engelke, J.1    Rüterjans, H.2
  • 8
    • 9444245493 scopus 로고
    • Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR
    • Grzesiek S, Bax A. 1992. Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR. J Am Chem Soc 114:6291-6293.
    • (1992) J Am Chem Soc , vol.114 , pp. 6291-6293
    • Grzesiek, S.1    Bax, A.2
  • 10
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert P, Mumenthaler C, Wüthrich K. 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
  • 11
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm L, Sander C. 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
  • 12
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay LE, Keifer P, Saarinen T. 1992. Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663-10665.
    • (1992) J Am Chem Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 14
    • 0028211605 scopus 로고
    • DNA replication: Enzymology and mechanisms
    • Kelman Z, O'Donnell M. 1994. DNA replication: Enzymology and mechanisms. Curr Opin Genet Dev 4:185-195.
    • (1994) Curr Opin Genet Dev , vol.4 , pp. 185-195
    • Kelman, Z.1    O'Donnell, M.2
  • 16
    • 0028545648 scopus 로고
    • α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods
    • α J couplings in calcium-free calmodulin using new 2D and 3D water-flip-back methods. J Biomol NMR 4:871-878.
    • (1994) J Biomol NMR , vol.4 , pp. 871-878
    • Kuboniwa, H.1    Grzesiek, S.2    Delaglio, F.3    Bax, A.4
  • 18
    • 0033168004 scopus 로고    scopus 로고
    • A preliminary CD and NMR study of the Escherichia coli DNA polymerase III θ subunit
    • Li D, Allen DL, Harvey S, Perrino FW, Schaaper RM, London RE. 1999. A preliminary CD and NMR study of the Escherichia coli DNA polymerase III θ subunit. Proteins 36:111-116.
    • (1999) Proteins , vol.36 , pp. 111-116
    • Li, D.1    Allen, D.L.2    Harvey, S.3    Perrino, F.W.4    Schaaper, R.M.5    London, R.E.6
  • 19
    • 0343607634 scopus 로고    scopus 로고
    • Unambiguous NOE assignments in proteins by a combination of through-bond and through-space correlations
    • Löhr F, Rüterjans H. 1997. Unambiguous NOE assignments in proteins by a combination of through-bond and through-space correlations. J Biomol NMR 9:371-378.
    • (1997) J Biomol NMR , vol.9 , pp. 371-378
    • Löhr, F.1    Rüterjans, H.2
  • 20
    • 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, Horiuchi T, Kornberg A. 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
  • 21
    • 0022345854 scopus 로고
    • The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the α subunit, devoid of nuclease activities
    • Maki H, Kornberg A. 1985. The polymerase subunit of DNA polymerase III of Escherichia coli. II. Purification of the α subunit, devoid of nuclease activities. J Biol Chem 260:12987-12992.
    • (1985) J Biol Chem , vol.260 , pp. 12987-12992
    • Maki, H.1    Kornberg, A.2
  • 23
    • 0023925456 scopus 로고
    • DNA polymerase III holoenzyme of Escherichia coli
    • McHenry CS. 1988. DNA polymerase III holoenzyme of Escherichia coli. Annu Rev Biochem 57:519-550.
    • (1988) Annu Rev Biochem , vol.57 , pp. 519-550
    • McHenry, C.S.1
  • 24
    • 0025997154 scopus 로고
    • DNA polymerase III holoenzyme: Component structure and mechanism of a true replicative complex
    • McHenry CS. 1991. DNA polymerase III holoenzyme: Component structure and mechanism of a true replicative complex. J Biol Chem 266:19127-19130.
    • (1991) J Biol Chem , vol.266 , pp. 19127-19130
    • McHenry, C.S.1
  • 26
    • 0028860964 scopus 로고
    • Improved RNA structure determination by detection of NOE contacts to exchange-broadened amino protons
    • Mueller L, Legault P, Pardi A. 1995. Improved RNA structure determination by detection of NOE contacts to exchange-broadened amino protons. J Am Chem Soc 117:11043-11048.
    • (1995) J Am Chem Soc , vol.117 , pp. 11043-11048
    • Mueller, L.1    Legault, P.2    Pardi, A.3
  • 27
    • 0001689741 scopus 로고
    • Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity
    • Muhandiram DR, Kay LE. 1994. Gradient-enhanced triple-resonance three-dimensional NMR experiments with improved sensitivity. J Magn Reson Ser B 103:203-216.
    • (1994) J Magn Reson Ser B , vol.103 , pp. 203-216
    • Muhandiram, D.R.1    Kay, L.E.2
  • 29
    • 0022347158 scopus 로고
    • Dynamics of DNA polymerase III holoenzyme of Escherichia coli in replication of a multiprimed template
    • O'Donnell ME, Kornberg A. 1985. Dynamics of DNA polymerase III holoenzyme of Escherichia coli in replication of a multiprimed template. J Biol Chem 260:12875-12883.
    • (1985) J Biol Chem , vol.260 , pp. 12875-12883
    • O'Donnell, M.E.1    Kornberg, A.2
  • 31
    • 0029817866 scopus 로고    scopus 로고
    • Crystal structure of human polymerase β complexed with DNA: Implications for catalytic mechanism, processivity and fidelity
    • Pelletier H, Sawaya MR, Wolfle W, Wilson SH, Kraut J. 1996. Crystal structure of human polymerase β complexed with DNA: Implications for catalytic mechanism, processivity and fidelity. Biochemistry 35:12742-12761.
    • (1996) Biochemistry , vol.35 , pp. 12742-12761
    • Pelletier, H.1    Sawaya, M.R.2    Wolfle, W.3    Wilson, S.H.4    Kraut, J.5
  • 32
    • 0019873820 scopus 로고
    • Estimation of globular protein secondary structure from circular dichroism
    • Provencher SW, Glöckner J. 1981. Estimation of globular protein secondary structure from circular dichroism. Biochemistry 20:33-37.
    • (1981) Biochemistry , vol.20 , pp. 33-37
    • Provencher, S.W.1    Glöckner, J.2
  • 33
    • 0020981110 scopus 로고
    • Identification of the ∈-subunit of Escherichia coli DNA polymerase III holoenzyme as the dnaQ gene product: A fidelity subunit for DNA replication
    • Scheuermann RH, Tam S, Burgers PMJ, Echols H. 1983. Identification of the ∈-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
  • 35
    • 0025988893 scopus 로고
    • Constitution of the twin polymerase of DNA polymerase III holoenzyme
    • Studwell-Vaughan PS, O'Donnell M. 1991. Constitution of the twin polymerase of DNA polymerase III holoenzyme. J Biol Chem 266:19833-19841.
    • (1991) J Biol Chem , vol.266 , pp. 19833-19841
    • Studwell-Vaughan, P.S.1    O'Donnell, M.2
  • 36
    • 0027158172 scopus 로고
    • DNA polymerase III accessory proteins, V. θ encoded by holE
    • Studwell-Vaughan PS, O'Donnell M. 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
  • 37
    • 44049114111 scopus 로고
    • Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets
    • Szyperski T, Güntert P, Otting G, Wüthrich K. 1992. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. J Magn Reson 99:552-560.
    • (1992) J Magn Reson , vol.99 , pp. 552-560
    • Szyperski, T.1    Güntert, P.2    Otting, G.3    Wüthrich, K.4
  • 38
  • 40
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • Wishart DS, Sykes BD. 1994b. 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
  • 42
    • 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.