메뉴 건너뛰기




Volumn 5, Issue 1, 2013, Pages 25-29

Direct Visualization of DNA Recognition by Restriction Endonuclease EcoRI

Author keywords

Optical tweezers; Quantum dots; Restriction endonucleases; Single molecule fluorescence detection; Single molecule manipulation

Indexed keywords

DOUBLE STRANDED DNA; QUANTUM DOT; RESTRICTION ENDONUCLEASE;

EID: 84875265412     PISSN: 18783317     EISSN: 18783325     Source Type: Journal    
DOI: 10.1016/j.jecm.2013.01.007     Document Type: Article
Times cited : (2)

References (20)
  • 1
    • 0024322164 scopus 로고
    • Discrimination between DNA sequences by the EcoRV restriction endonuclease
    • Taylor J.D., Halford S.E. Discrimination between DNA sequences by the EcoRV restriction endonuclease. Biochemistry 1989, 28:6198-6207.
    • (1989) Biochemistry , vol.28 , pp. 6198-6207
    • Taylor, J.D.1    Halford, S.E.2
  • 2
    • 0027159254 scopus 로고
    • The crystal structure of EcoRV endonuclease and of its complexes with cognate and noncognate DNA fragments
    • Winkler F.K., Banner D.W., Oefner C., Tsernoglou D., Brown R.S., Heathman S.P., Bryan R.K., et al. The crystal structure of EcoRV endonuclease and of its complexes with cognate and noncognate DNA fragments. EMBO J 1993, 12:1781-1795.
    • (1993) EMBO J , vol.12 , pp. 1781-1795
    • Winkler, F.K.1    Banner, D.W.2    Oefner, C.3    Tsernoglou, D.4    Brown, R.S.5    Heathman, S.P.6    Bryan, R.K.7
  • 3
    • 0033634983 scopus 로고    scopus 로고
    • Structure of BamHI bound to nonspecific DNA: a model for DNA sliding
    • Viadiu H., Aggarwal A.K. Structure of BamHI bound to nonspecific DNA: a model for DNA sliding. Mol Cell 2000, 5:889-895.
    • (2000) Mol Cell , vol.5 , pp. 889-895
    • Viadiu, H.1    Aggarwal, A.K.2
  • 6
    • 33845353937 scopus 로고    scopus 로고
    • Dynamics of single DNA looping and cleavage by Sau3AI and effect of tension applied to the DNA
    • Gemmen G.J., Millin R., Smith D.E. Dynamics of single DNA looping and cleavage by Sau3AI and effect of tension applied to the DNA. Biophys J 2006, 91:4154-4165.
    • (2006) Biophys J , vol.91 , pp. 4154-4165
    • Gemmen, G.J.1    Millin, R.2    Smith, D.E.3
  • 7
    • 33744546367 scopus 로고    scopus 로고
    • DNA looping by two-site restriction endonucleases: heterogeneous probability distributions for loop size and unbinding force
    • Gemmen G.J., Millin R., Smith D.E. DNA looping by two-site restriction endonucleases: heterogeneous probability distributions for loop size and unbinding force. Nucleic Acids Res 2006, 34:2864-2877.
    • (2006) Nucleic Acids Res , vol.34 , pp. 2864-2877
    • Gemmen, G.J.1    Millin, R.2    Smith, D.E.3
  • 9
    • 0037451299 scopus 로고    scopus 로고
    • Protein motion from non-specific to specific DNA by three-dimensional routes aided by supercoiling
    • Gowers D.M., Halford S.E. Protein motion from non-specific to specific DNA by three-dimensional routes aided by supercoiling. EMBO J 2003, 22:1410-1418.
    • (2003) EMBO J , vol.22 , pp. 1410-1418
    • Gowers, D.M.1    Halford, S.E.2
  • 10
    • 3042579602 scopus 로고    scopus 로고
    • How do site-specific DNA-binding proteins find their targets?
    • Halford S.E., Marko J.F. How do site-specific DNA-binding proteins find their targets?. Nucleic Acids Res 2004, 32:3040-3052.
    • (2004) Nucleic Acids Res , vol.32 , pp. 3040-3052
    • Halford, S.E.1    Marko, J.F.2
  • 11
    • 0034387984 scopus 로고    scopus 로고
    • One- and three-dimensional pathways for proteins to reach specific DNA sites
    • Stanford N.P., Szczelkun M.D., Marko J.F., Halford S.E. One- and three-dimensional pathways for proteins to reach specific DNA sites. EMBO J 2000, 19:6546-6557.
    • (2000) EMBO J , vol.19 , pp. 6546-6557
    • Stanford, N.P.1    Szczelkun, M.D.2    Marko, J.F.3    Halford, S.E.4
  • 12
    • 0036656143 scopus 로고    scopus 로고
    • How to get from A to B: strategies for analyzing protein motion on DNA
    • Halford S.E., Szczelkun M.D. How to get from A to B: strategies for analyzing protein motion on DNA. Eur Biophys J 2002, 31:257-267.
    • (2002) Eur Biophys J , vol.31 , pp. 257-267
    • Halford, S.E.1    Szczelkun, M.D.2
  • 13
    • 33746824311 scopus 로고    scopus 로고
    • Tension-dependent DNA cleavage by restriction endonucleases: two-site enzymes are "switched off" at low force
    • Gemmen G.J., Millin R., Smith D.E. Tension-dependent DNA cleavage by restriction endonucleases: two-site enzymes are "switched off" at low force. Proc Natl Acad Sci USA 2006, 103:11555-11560.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 11555-11560
    • Gemmen, G.J.1    Millin, R.2    Smith, D.E.3
  • 14
    • 19444384194 scopus 로고    scopus 로고
    • DNA-tension dependence of restriction enzyme activity reveals mechanochemical properties of the reaction pathway
    • van den Broek B., Noom M.C., Wuite G.J.L. DNA-tension dependence of restriction enzyme activity reveals mechanochemical properties of the reaction pathway. Nucleic Acids Res 2005, 33:2676-2684.
    • (2005) Nucleic Acids Res , vol.33 , pp. 2676-2684
    • van den Broek, B.1    Noom, M.C.2    Wuite, G.J.L.3
  • 15
    • 0034194282 scopus 로고    scopus 로고
    • Probing specific sequences on single DNA molecules with bioconjugated fluorescent nanoparticles
    • Taylor J.R., Fang M.M., Nie S. Probing specific sequences on single DNA molecules with bioconjugated fluorescent nanoparticles. Anal Chem 2000, 72:1979-1986.
    • (2000) Anal Chem , vol.72 , pp. 1979-1986
    • Taylor, J.R.1    Fang, M.M.2    Nie, S.3
  • 16
    • 70350761899 scopus 로고    scopus 로고
    • Determining the zero-force binding energetics of an intercalated DNA complex by a single-molecule approach
    • Yang T.S., Cui Y., Wu C.M., Lo J.M., Chiang C.S., Shu W.Y., Chung W.J., et al. Determining the zero-force binding energetics of an intercalated DNA complex by a single-molecule approach. Chemphyschem 2009, 10:2791-2794.
    • (2009) Chemphyschem , vol.10 , pp. 2791-2794
    • Yang, T.S.1    Cui, Y.2    Wu, C.M.3    Lo, J.M.4    Chiang, C.S.5    Shu, W.Y.6    Chung, W.J.7
  • 17
    • 78650911204 scopus 로고    scopus 로고
    • Determining the binding mode and binding affinity constant of tyrosine kinase inhibitor PD153035 to DNA using optical tweezers
    • Cheng C.M., Lee Y.J., Wang W.T., Hsu C.T., Tsai J.S., Wu C.M., Ou K.L., et al. Determining the binding mode and binding affinity constant of tyrosine kinase inhibitor PD153035 to DNA using optical tweezers. Biochem Biophys Res Commun 2011, 404:297-301.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 297-301
    • Cheng, C.M.1    Lee, Y.J.2    Wang, W.T.3    Hsu, C.T.4    Tsai, J.S.5    Wu, C.M.6    Ou, K.L.7
  • 18
    • 0036284131 scopus 로고    scopus 로고
    • An automated two-dimensional optical force clamp for single molecule studies
    • Lang J.M., Asbury C.L., Shaevits J.W., Block S.M. An automated two-dimensional optical force clamp for single molecule studies. Biophys J 2002, 83:491-501.
    • (2002) Biophys J , vol.83 , pp. 491-501
    • Lang, J.M.1    Asbury, C.L.2    Shaevits, J.W.3    Block, S.M.4
  • 19
    • 0037091515 scopus 로고    scopus 로고
    • Three-dimensional position detection of optically trapped dielectric particles
    • Rohrbach A., Stelzer E.H. Three-dimensional position detection of optically trapped dielectric particles. J Appl Phys 2002, 91:5474-5488.
    • (2002) J Appl Phys , vol.91 , pp. 5474-5488
    • Rohrbach, A.1    Stelzer, E.H.2
  • 20
    • 15944386330 scopus 로고    scopus 로고
    • Two-way interaction between solid particles and homogeneous air turbulence: particle settling rate and turbulence modification measurements
    • Yang T.S., Shy S.S. Two-way interaction between solid particles and homogeneous air turbulence: particle settling rate and turbulence modification measurements. J Fluid Mech 2005, 526:171-216.
    • (2005) J Fluid Mech , vol.526 , pp. 171-216
    • Yang, T.S.1    Shy, S.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.