메뉴 건너뛰기




Volumn 310, Issue 4, 2003, Pages 1096-1103

The impact of single cysteine residue mutations on the replication terminator protein

Author keywords

Bacillus subtilis; Biophysical analysis; Cysteine mutagenesis; DNA binding; Protein engineering; Protein structure and function; Replication terminator protein

Indexed keywords

ALANINE; CYSTEINE; MUTANT PROTEIN; PROTEIN; REPLICATION TERMINATOR PROTEIN; SERINE; UNCLASSIFIED DRUG; VALINE;

EID: 0141961674     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.09.126     Document Type: Article
Times cited : (10)

References (22)
  • 1
    • 0000384235 scopus 로고    scopus 로고
    • Features of the chromosomal terminus region
    • F.C. Neidhardt, R. Curtiss III, J.L. Ingraham, E.C. Lin, K.B. Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, & H.E. Umbarger. Washington, DC: American Society for Microbiology
    • Hill T.M. Features of the chromosomal terminus region. Neidhardt F.C., Curtiss III R., Ingraham J.L., Lin E.C., Low K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella: Cellular and Molecular Biology. 1996;1602-1614 American Society for Microbiology, Washington, DC.
    • (1996) Escherichia coli and Salmonella: Cellular and Molecular Biology , pp. 1602-1614
    • Hill, T.M.1
  • 2
    • 0030740823 scopus 로고    scopus 로고
    • Replication fork arrest and termination of chromosome replication in Bacillus subtilis
    • Wake R.G. Replication fork arrest and termination of chromosome replication in Bacillus subtilis. FEMS Microbiol. Lett. 153:1997;247-254.
    • (1997) FEMS Microbiol. Lett. , vol.153 , pp. 247-254
    • Wake, R.G.1
  • 3
    • 0031568338 scopus 로고    scopus 로고
    • A tale of two terminators: Crystal structures sharpen the debate on DNA replication fork arrest mechanisms
    • Wake R.G., King G.F. A tale of two terminators: crystal structures sharpen the debate on DNA replication fork arrest mechanisms. Structure. 5:1997;1-5.
    • (1997) Structure , vol.5 , pp. 1-5
    • Wake, R.G.1    King, G.F.2
  • 4
    • 0031779299 scopus 로고    scopus 로고
    • Replication terminator protein-based replication fork-arrest systems in various Bacillus species
    • Griffiths A.A., Anderson, Wake R.G. Replication terminator protein-based replication fork-arrest systems in various Bacillus species. J. Bacteriol. 180:1998;3360-3367.
    • (1998) J. Bacteriol. , vol.180 , pp. 3360-3367
    • Griffiths, A.A.1    Anderson2    Wake, R.G.3
  • 5
    • 0030835634 scopus 로고    scopus 로고
    • Reorganisation of terminator DNA upon binding replication terminator protein: Implications for the functional fork arrest complex
    • Kralicek A.V., Wilson P.K., Ralston G.B., Wake R.G., King G.F. Reorganisation of terminator DNA upon binding replication terminator protein: implications for the functional fork arrest complex. Nucleic Acids Res. 25:1997;590-596.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 590-596
    • Kralicek, A.V.1    Wilson, P.K.2    Ralston, G.B.3    Wake, R.G.4    King, G.F.5
  • 7
    • 0027494868 scopus 로고
    • Symmetry and secondary structure of the replication terminator protein of Bacillus subtilis: Sedimentation equilibrium and circular dichroic, infrared, and NMR spectroscopic studies
    • Kralicek A.V., Vesper N.A., Ralston G.B., Wake R.G., King G.F. Symmetry and secondary structure of the replication terminator protein of Bacillus subtilis: sedimentation equilibrium and circular dichroic, infrared, and NMR spectroscopic studies. Biochemistry. 32:1993;10216-10223.
    • (1993) Biochemistry , vol.32 , pp. 10216-10223
    • Kralicek, A.V.1    Vesper, N.A.2    Ralston, G.B.3    Wake, R.G.4    King, G.F.5
  • 8
    • 0001038767 scopus 로고
    • Equilibrium ultracentrifugation of dilute solutions
    • Yphantis D.A. Equilibrium ultracentrifugation of dilute solutions. Biochemistry. 3:1964;297-317.
    • (1964) Biochemistry , vol.3 , pp. 297-317
    • Yphantis, D.A.1
  • 9
    • 0019756004 scopus 로고
    • Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques
    • Johnson M.L., Correia J.J., Yphantis D.A., Halvorson H.R. Analysis of data from the analytical ultracentrifuge by nonlinear least-squares techniques. Biophys. J. 36:1981;575-588.
    • (1981) Biophys. J. , vol.36 , pp. 575-588
    • Johnson, M.L.1    Correia, J.J.2    Yphantis, D.A.3    Halvorson, H.R.4
  • 11
    • 0033548584 scopus 로고    scopus 로고
    • Site-directed mutants of RTP of Bacillus subtilis and the mechanism of replication fork arrest
    • Duggin I.G., Anderson P.A., Smith M.T., Wilce J.A., King G.F., Wake R.G. Site-directed mutants of RTP of Bacillus subtilis and the mechanism of replication fork arrest. J. Mol. Biol. 286:1999;1325-1335.
    • (1999) J. Mol. Biol. , vol.286 , pp. 1325-1335
    • Duggin, I.G.1    Anderson, P.A.2    Smith, M.T.3    Wilce, J.A.4    King, G.F.5    Wake, R.G.6
  • 12
    • 0026753495 scopus 로고
    • Crystallisation ond preliminary structural analysis of the replicator terminator protein of Bacillus subtilis
    • Mehta P.P., Bussierre D.E., Hoffman D.W., Bastia D., White S.W. Crystallisation ond preliminary structural analysis of the replicator terminator protein of Bacillus subtilis. J. Biol. Chem. 267:1992;18885-18889.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18885-18889
    • Mehta, P.P.1    Bussierre, D.E.2    Hoffman, D.W.3    Bastia, D.4    White, S.W.5
  • 13
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z., Minor W. Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol. 276:1997;307-326.
    • (1997) Methods Enzymol. , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 14
    • 0028103275 scopus 로고
    • The CCP4 Suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4, The CCP4 Suite: programs for protein crystallography, Acta Cryst. D 50 (1994) 760-763.
    • (1994) Acta Cryst. D , vol.50 , pp. 760-763
  • 15
    • 0028918469 scopus 로고
    • Crystal structure of the replication terminator protein from B. subtilis at 2.6 Å
    • Bussiere D.E., Bastia D., White S.W. Crystal structure of the replication terminator protein from B. subtilis at 2.6. Å Cell. 80:1995;651-660.
    • (1995) Cell , vol.80 , pp. 651-660
    • Bussiere, D.E.1    Bastia, D.2    White, S.W.3
  • 17
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zou J.-Y., Cowan S.W., Kjeldgaard M. Improved methods for building protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 18
    • 45149138663 scopus 로고
    • Comparison of different modes of two-dimensional reverse correlation NMR for the study of proteins
    • Bax A., Ikura M., Kay L.E., Torchia D.A., Tschudin R. Comparison of different modes of two-dimensional reverse correlation NMR for the study of proteins. J. Magn. Reson. 86:1990;304-318.
    • (1990) J. Magn. Reson. , vol.86 , pp. 304-318
    • Bax, A.1    Ikura, M.2    Kay, L.E.3    Torchia, D.A.4    Tschudin, R.5
  • 20
    • 0030005544 scopus 로고    scopus 로고
    • The structure and function of the replication terminator protein of Bacillus subtilis: Identification of the 'winged helix' DNA-binding domain
    • Pai K.S., Bussiere D.E., Wang F., Hutchison III C.A., White S.W., Bastia D. The structure and function of the replication terminator protein of Bacillus subtilis: identification of the 'winged helix' DNA-binding domain. EMBO J. 15:1996;3164-3173.
    • (1996) EMBO J. , vol.15 , pp. 3164-3173
    • Pai, K.S.1    Bussiere, D.E.2    Wang, F.3    Hutchison C.A. III4    White, S.W.5    Bastia, D.6
  • 21
    • 0023290578 scopus 로고
    • Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cystochrome c with threonine: Improved stability of the mutant protein
    • Cutler R.L., Pielak G.J., Mauk A.G., Smith M. Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cystochrome c with threonine: improved stability of the mutant protein. Protein Eng. 1:1987;95-99.
    • (1987) Protein Eng. , vol.1 , pp. 95-99
    • Cutler, R.L.1    Pielak, G.J.2    Mauk, A.G.3    Smith, M.4
  • 22
    • 0028147704 scopus 로고
    • Role of cysteine residues in esterase from Bacillus stearothermophilus and increasing its thermostability by the replacement of cysteines
    • Amaki Y., Nakano H., Yamane T. Role of cysteine residues in esterase from Bacillus stearothermophilus and increasing its thermostability by the replacement of cysteines. Appl. Microbiol. Biotechnol. 40:1994;664-668.
    • (1994) Appl. Microbiol. Biotechnol. , vol.40 , pp. 664-668
    • Amaki, Y.1    Nakano, H.2    Yamane, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.