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Volumn 40, Issue 13, 2012, Pages 6208-6222

Real-time single-molecule tethered particle motion experiments reveal the kinetics and mechanisms of Cre-mediated site-specific recombination

Author keywords

[No Author keywords available]

Indexed keywords

CRE RECOMBINASE; DIVALENT CATION; DNA; MONOVALENT CATION; NUCLEOPROTEIN;

EID: 84864482180     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gks274     Document Type: Article
Times cited : (39)

References (47)
  • 1
    • 0022596135 scopus 로고
    • Copy number amplification of the 2 micron circle plasmid of saccharomyces cerevisiae
    • Futcher, A.B. (1986) Copy number amplification of the 2 micron circle plasmid of Saccharomyces cerevisiae. J. Theor. Biol., 119, 197-204.
    • (1986) J. Theor. Biol. , vol.119 , pp. 197-204
    • Futcher, A.B.1
  • 3
    • 0030133847 scopus 로고    scopus 로고
    • Architectural flexibility in lambda site-specific recombination: Three alternate conformations channel the attl site into three distinct pathways
    • Segall, A.M. and Nash, H.A. (1996) Architectural flexibility in lambda site-specific recombination: three alternate conformations channel the attL site into three distinct pathways. Genes Cells, 1, 453-463.
    • (1996) Genes Cells , vol.1 , pp. 453-463
    • Segall, A.M.1    Nash, H.A.2
  • 5
    • 0030816550 scopus 로고    scopus 로고
    • The integrase family of tyrosine recombinases: Evolution of a conserved active site domain
    • Esposito, D. and Scocca, J.J. (1997) The integrase family of tyrosine recombinases: evolution of a conserved active site domain. Nucleic Acids Res., 25, 3605-3614.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 3605-3614
    • Esposito, D.1    Scocca, J.J.2
  • 6
    • 0036235348 scopus 로고    scopus 로고
    • Genome engineering using site-specific recombinases
    • Kolb, A.F. (2002) Genome engineering using site-specific recombinases. Cloning Stem Cells, 4, 65-80.
    • (2002) Cloning Stem Cells , vol.4 , pp. 65-80
    • Kolb, A.F.1
  • 7
    • 0029155706 scopus 로고
    • Inducible gene targeting in mice
    • Kuhn, R., Schwenk, F., Aguet, M. and Rajewsky, K. (1995) Inducible gene targeting in mice. Science, 269, 1427-1429.
    • (1995) Science , vol.269 , pp. 1427-1429
    • Kuhn, R.1    Schwenk, F.2    Aguet, M.3    Rajewsky, K.4
  • 8
    • 0033644144 scopus 로고    scopus 로고
    • Conditional gene knockout using cre recombinase
    • Le, Y. and Sauer, B. (2000) Conditional gene knockout using cre recombinase. Methods Mol. Biol., 136, 477-485.
    • (2000) Methods Mol. Biol. , vol.136 , pp. 477-485
    • Le, Y.1    Sauer, B.2
  • 9
    • 0020397021 scopus 로고
    • Site-specific DNA condensation and pairing mediated by the int protein of bacteriophage lambda
    • Better, M., Lu, C., Williams, R.C. and Echols, H. (1982) Site-specific DNA condensation and pairing mediated by the int protein of bacteriophage lambda. Proc. Natl Acad. Sci. USA, 79, 5837-5841.
    • (1982) Proc. Natl Acad. Sci. USA , vol.79 , pp. 5837-5841
    • Better, M.1    Lu, C.2    Williams, R.C.3    Echols, H.4
  • 10
    • 0021764162 scopus 로고
    • Site-specific recombination by the bacteriophage P1 lox-cre system. Cre-mediated synapsis of two lox sites
    • Hamilton, D.L. and Abremski, K. (1984) Site-specific recombination by the bacteriophage P1 lox-Cre system. Cre-mediated synapsis of two lox sites. J. Mol. Biol., 178, 481-486.
    • (1984) J. Mol. Biol. , vol.178 , pp. 481-486
    • Hamilton, D.L.1    Abremski, K.2
  • 11
    • 0027422131 scopus 로고
    • Synaptic intermediates in bacteriophage lambda site-specific recombination: Integrase can align pairs of attachment sites
    • Segall, A.M. and Nash, H.A. (1993) Synaptic intermediates in bacteriophage lambda site-specific recombination: integrase can align pairs of attachment sites. EMBO J., 12, 4567-4576.
    • (1993) EMBO J. , vol.12 , pp. 4567-4576
    • Segall, A.M.1    Nash, H.A.2
  • 12
    • 34548261888 scopus 로고    scopus 로고
    • Synapsis of loxp sites by cre recombinase
    • Ghosh, K., Guo, F. and Van Duyne, G.D. (2007) Synapsis of loxP sites by Cre recombinase. J. Biol. Chem., 282, 24004-24016.
    • (2007) J. Biol. Chem. , vol.282 , pp. 24004-24016
    • Ghosh, K.1    Guo, F.2    Van Duyne, G.D.3
  • 13
    • 0030886293 scopus 로고    scopus 로고
    • Structure of cre recombinase complexed with DNA in a site-specific recombination synapse
    • Guo, F., Gopaul, D.N. and van Duyne, G.D. (1997) Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Nature, 389, 40-46.
    • (1997) Nature , vol.389 , pp. 40-46
    • Guo, F.1    Gopaul, D.N.2    Van Duyne, G.D.3
  • 15
    • 0033557229 scopus 로고    scopus 로고
    • The geometry of a synaptic intermediate in a pathway of bacteriophage lambda site-specific recombination
    • Cassell, G., Moision, R., Rabani, E. and Segall, A. (1999) The geometry of a synaptic intermediate in a pathway of bacteriophage lambda site-specific recombination. Nucleic Acids Res., 27, 1145-1151.
    • (1999) Nucleic Acids Res. , vol.27 , pp. 1145-1151
    • Cassell, G.1    Moision, R.2    Rabani, E.3    Segall, A.4
  • 16
    • 0033594916 scopus 로고    scopus 로고
    • Asymmetric DNA bending in the Cre-loxP site-specific recombination synapse
    • Guo, F., Gopaul, D.N. and Van Duyne, G.D. (1999) Asymmetric DNA bending in the Cre-loxP site-specific recombination synapse. Proc. Natl Acad. Sci. USA, 96, 7143-7148.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 7143-7148
    • Guo, F.1    Gopaul, D.N.2    Van Duyne, G.D.3
  • 17
    • 0344012172 scopus 로고    scopus 로고
    • Crystal structure of a wild-type cre recombinase-loxp synapse reveals a novel spacer conformation suggesting an alternative mechanism for DNA cleavage activation
    • Ennifar, E., Meyer, J.E., Buchholz, F., Stewart, A.F. and Suck, D. (2003) Crystal structure of a wild-type Cre recombinase-loxP synapse reveals a novel spacer conformation suggesting an alternative mechanism for DNA cleavage activation. Nucleic Acids Res., 31, 5449-5460.
    • (2003) Nucleic Acids Res. , vol.31 , pp. 5449-5460
    • Ennifar, E.1    Meyer, J.E.2    Buchholz, F.3    Stewart, A.F.4    Suck, D.5
  • 18
    • 0036751010 scopus 로고    scopus 로고
    • Analysis of cre-loxp interaction by surface plasmon resonance: Influence of spermidine on cooperativity
    • Rufer, A., Neuenschwander, P.F. and Sauer, B. (2002) Analysis of Cre-loxP interaction by surface plasmon resonance: influence of spermidine on cooperativity. Anal. Biochem., 308, 90-99.
    • (2002) Anal. Biochem. , vol.308 , pp. 90-99
    • Rufer, A.1    Neuenschwander, P.F.2    Sauer, B.3
  • 19
    • 33749359386 scopus 로고    scopus 로고
    • Viewing single lambda site-specific recombination events from start to finish
    • Mumm, J.P., Landy, A. and Gelles, J. (2006) Viewing single lambda site-specific recombination events from start to finish. EMBO J., 25, 4586-4595.
    • (2006) EMBO J. , vol.25 , pp. 4586-4595
    • Mumm, J.P.1    Landy, A.2    Gelles, J.3
  • 20
    • 79956326013 scopus 로고    scopus 로고
    • Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine recombinase
    • Bai, H., Sun, M., Ghosh, P., Hatfull, G.F., Grindley, N.D. and Marko, J.F. (2011) Single-molecule analysis reveals the molecular bearing mechanism of DNA strand exchange by a serine recombinase. Proc. Natl Acad. Sci. USA, 108, 7419-7424.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , pp. 7419-7424
    • Bai, H.1    Sun, M.2    Ghosh, P.3    Hatfull, G.F.4    Grindley, N.D.5    Marko, J.F.6
  • 21
    • 0023659915 scopus 로고
    • Isolation of intermediates in the binding of the FLP recombinase of the yeast plasmid 2-Micron circle to its target sequence
    • Andrews, B.J., Beatty, L.G. and Sadowski, P.D. (1987) Isolation of intermediates in the binding of the FLP recombinase of the yeast plasmid 2-micron circle to its target sequence. J. Mol. Biol., 193, 345-358.
    • (1987) J. Mol. Biol. , vol.193 , pp. 345-358
    • Andrews, B.J.1    Beatty, L.G.2    Sadowski, P.D.3
  • 22
    • 0005673882 scopus 로고
    • Interaction of the bacteriophage P1 recombinase cre with the recombining site loxp
    • Hoess, R.H. and Abremski, K. (1984) Interaction of the bacteriophage P1 recombinase Cre with the recombining site loxP. Proc. Natl Acad. Sci. USA, 81, 1026-1029.
    • (1984) Proc. Natl Acad. Sci. USA , vol.81 , pp. 1026-1029
    • Hoess, R.H.1    Abremski, K.2
  • 23
    • 0026731049 scopus 로고
    • Stoichiometry of the cre recombinase bound to the lox recombining site
    • Mack, A., Sauer, B., Abremski, K. and Hoess, R. (1992) Stoichiometry of the Cre recombinase bound to the lox recombining site. Nucleic Acids Res., 20, 4451-4455.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 4451-4455
    • Mack, A.1    Sauer, B.2    Abremski, K.3    Hoess, R.4
  • 24
    • 0023053303 scopus 로고
    • FLP site-specific recombinase of yeast 2-Micron plasmid. Topological features of the reaction
    • Beatty, L.G., Babineau-Clary, D., Hogrefe, C. and Sadowski, P.D. (1986) FLP site-specific recombinase of yeast 2-micron plasmid. Topological features of the reaction. J. Mol. Biol., 188, 529-544.
    • (1986) J. Mol. Biol. , vol.188 , pp. 529-544
    • Beatty, L.G.1    Babineau-Clary, D.2    Hogrefe, C.3    Sadowski, P.D.4
  • 25
    • 0021245666 scopus 로고
    • Bacteriophage P1 site-specific recombination. Purification and properties of the cre recombinase protein
    • Abremski, K. and Hoess, R. (1984) Bacteriophage P1 site-specific recombination. Purification and properties of the Cre recombinase protein. J. Biol. Chem., 259, 1509-1514.
    • (1984) J. Biol. Chem. , vol.259 , pp. 1509-1514
    • Abremski, K.1    Hoess, R.2
  • 26
    • 0026784978 scopus 로고
    • Cre-lox recombination in escherichia coli cells
    • Adams, D.E., Bliska, J.B. and Cozzarelli, N.R. (1992) Cre-lox recombination in Escherichia coli cells. J. Mol. Biol., 226, 661-673.
    • (1992) J. Mol. Biol. , vol.226 , pp. 661-673
    • Adams, D.E.1    Bliska, J.B.2    Cozzarelli, N.R.3
  • 28
    • 0028799019 scopus 로고
    • A protein dissociation step limits turnover in FLP recombinase-mediated site-specific recombination
    • Waite, L.L. and Cox, M.M. (1995) A protein dissociation step limits turnover in FLP recombinase-mediated site-specific recombination. J. Biol. Chem., 270, 23409-23414.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23409-23414
    • Waite, L.L.1    Cox, M.M.2
  • 29
    • 70350488396 scopus 로고    scopus 로고
    • SSB protein diffusion on single-stranded DNA stimulates RecA filament formation
    • Roy, R., Kozlov, A.G., Lohman, T.M. and Ha, T. (2009) SSB protein diffusion on single-stranded DNA stimulates RecA filament formation. Nature, 461, 1092-1097.
    • (2009) Nature , vol.461 , pp. 1092-1097
    • Roy, R.1    Kozlov, A.G.2    Lohman, T.M.3    Ha, T.4
  • 30
    • 70349775652 scopus 로고    scopus 로고
    • An SOS inhibitor that binds to free RecA protein: The PsiB protein
    • Petrova, V., Chitteni-Pattu, S., Drees, J.C., Inman, R.B. and Cox, M.M. (2009) An SOS inhibitor that binds to free RecA protein: the PsiB protein. Mol. Cell, 36, 121-130.
    • (2009) Mol. Cell , vol.36 , pp. 121-130
    • Petrova, V.1    Chitteni-Pattu, S.2    Drees, J.C.3    Inman, R.B.4    Cox, M.M.5
  • 31
    • 0032573418 scopus 로고    scopus 로고
    • Comparative kinetic analysis of FLP and cre recombinases: Mathematical models for DNA binding and recombination
    • Ringrose, L., Lounnas, V., Ehrlich, L., Buchholz, F., Wade, R. and Stewart, A.F. (1998) Comparative kinetic analysis of FLP and cre recombinases: mathematical models for DNA binding and recombination. J. Mol. Biol., 284, 363-384.
    • (1998) J. Mol. Biol. , vol.284 , pp. 363-384
    • Ringrose, L.1    Lounnas, V.2    Ehrlich, L.3    Buchholz, F.4    Wade, R.5    Stewart, A.F.6
  • 32
    • 65549152342 scopus 로고    scopus 로고
    • Studying recbcd helicase translocation along chi-dna using tethered particle motion with a stretching force
    • Fan, H.F. and Li, H.W. (2009) Studying RecBCD helicase translocation along Chi-DNA using tethered particle motion with a stretching force. Biophys. J., 96, 1875-1883.
    • (2009) Biophys. J. , vol.96 , pp. 1875-1883
    • Fan, H.F.1    Li, H.W.2
  • 33
    • 79960164880 scopus 로고    scopus 로고
    • Developing singlemolecule TPM experiments for direct observation of successful RecA-mediated strand exchange reaction
    • Fan, H.F., Cox, M.M. and Li, H.W. (2011) Developing singlemolecule TPM experiments for direct observation of successful RecA-mediated strand exchange reaction. PLoS One, 6, e21359.
    • (2011) PLoS One , vol.6
    • Fan, H.F.1    Cox, M.M.2    Li, H.W.3
  • 34
    • 0036438816 scopus 로고    scopus 로고
    • Cre-loxp biochemistry
    • Ghosh, K. and Van Duyne, G.D. (2002) Cre-loxP biochemistry. Methods, 28, 374-383.
    • (2002) Methods , vol.28 , pp. 374-383
    • Ghosh, K.1    Van Duyne, G.D.2
  • 35
    • 79551504946 scopus 로고    scopus 로고
    • Probing DNA conformational changes with high temporal resolution by tethered particle motion
    • Manghi, M., Tardin, C., Baglio, J., Rousseau, P., Salome, L. and Destainville, N. (2010) Probing DNA conformational changes with high temporal resolution by tethered particle motion. Phys. Biol., 7, 046003.
    • (2010) Phys. Biol. , vol.7 , pp. 046003
    • Manghi, M.1    Tardin, C.2    Baglio, J.3    Rousseau, P.4    Salome, L.5    Destainville, N.6
  • 36
    • 77954571156 scopus 로고    scopus 로고
    • Quantitative analysis of dna-looping kinetics from tethered particle motion experiments
    • Manzo, C. and Finzi, L. (2010) Quantitative analysis of DNA-looping kinetics from tethered particle motion experiments. Methods Enzymol., 475, 199-220.
    • (2010) Methods Enzymol. , vol.475 , pp. 199-220
    • Manzo, C.1    Finzi, L.2
  • 38
    • 33746207766 scopus 로고    scopus 로고
    • Lac repressor hinge flexibility and DNA looping: Single molecule kinetics by tethered particle motion
    • Vanzi, F., Broggio, C., Sacconi, L. and Pavone, F.S. (2006) Lac repressor hinge flexibility and DNA looping: single molecule kinetics by tethered particle motion. Nucleic Acids Res., 34, 3409-3420.
    • (2006) Nucleic Acids Res. , vol.34 , pp. 3409-3420
    • Vanzi, F.1    Broggio, C.2    Sacconi, L.3    Pavone, F.S.4
  • 39
    • 0028143652 scopus 로고
    • Tethered particle motion method for studying transcript elongation by a single RNA polymerase molecule
    • Yin, H., Landick, R. and Gelles, J. (1994) Tethered particle motion method for studying transcript elongation by a single RNA polymerase molecule. Biophys. J., 67, 2468-2478.
    • (1994) Biophys. J. , vol.67 , pp. 2468-2478
    • Yin, H.1    Landick, R.2    Gelles, J.3
  • 40
    • 0023179984 scopus 로고
    • Homology-dependent interactions in phage lambda site-specific recombination
    • Kitts, P.A. and Nash, H.A. (1987) Homology-dependent interactions in phage lambda site-specific recombination. Nature, 329, 346-348.
    • (1987) Nature , vol.329 , pp. 346-348
    • Kitts, P.A.1    Nash, H.A.2
  • 42
    • 0028934112 scopus 로고
    • Specific DNA recognition by ecorv restriction endonuclease induced by calcium ions
    • Vipond, I.B. and Halford, S.E. (1995) Specific DNA recognition by EcoRV restriction endonuclease induced by calcium ions. Biochemistry, 34, 1113-1119.
    • (1995) Biochemistry , vol.34 , pp. 1113-1119
    • Vipond, I.B.1    Halford, S.E.2
  • 43
    • 0345055328 scopus 로고    scopus 로고
    • DNA bending by small, mobile multivalent cations
    • Rouzina, I. and Bloomfield, V.A. (1998) DNA bending by small, mobile multivalent cations. Biophys. J., 74, 3152-3164.
    • (1998) Biophys. J. , vol.74 , pp. 3152-3164
    • Rouzina, I.1    Bloomfield, V.A.2
  • 44
    • 0019867850 scopus 로고
    • Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The escherichia coli lac repressor-operator interaction: kinetic measurements and conclusions
    • Winter, R.B., Berg, O.G. and von Hippel, P.H. (1981) Diffusion-driven mechanisms of protein translocation on nucleic acids. 3. The Escherichia coli lac repressor-operator interaction: kinetic measurements and conclusions. Biochemistry, 20, 6961-6977.
    • (1981) Biochemistry , vol.20 , pp. 6961-6977
    • Winter, R.B.1    Berg, O.G.2    Von Hippel, P.H.3
  • 45
    • 0022573212 scopus 로고
    • Kinetics of protein-nucleic acid interactions: Use of salt effects to probe mechanisms of interaction
    • Lohman, T.M. (1986) Kinetics of protein-nucleic acid interactions: use of salt effects to probe mechanisms of interaction. CRC Crit. Rev. Biochem., 19, 191-245.
    • (1986) CRC Crit. Rev. Biochem. , vol.19 , pp. 191-245
    • Lohman, T.M.1
  • 46
    • 0037389327 scopus 로고    scopus 로고
    • Mutations at residues 282, 286, and 293 of phage lambda integrase exert pathway-specific effects on synapsis and catalysis in recombination
    • Bankhead, T.M., Etzel, B.J., Wolven, F., Bordenave, S., Boldt, J.L., Larsen, T.A. and Segall, A.M. (2003) Mutations at residues 282, 286, and 293 of phage lambda integrase exert pathway-specific effects on synapsis and catalysis in recombination. J. Bacteriol., 185, 2653-2666.
    • (2003) J. Bacteriol. , vol.185 , pp. 2653-2666
    • Bankhead, T.M.1    Etzel, B.J.2    Wolven, F.3    Bordenave, S.4    Boldt, J.L.5    Larsen, T.A.6    Segall, A.M.7


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