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Volumn 440, Issue 7088, 2006, Pages 1157-1162

Structural basis for broad DNA-specificity in integron recombination

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA; GENETIC ENGINEERING; PROTEINS;

EID: 33646337441     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature04643     Document Type: Article
Times cited : (129)

References (40)
  • 1
    • 1542513556 scopus 로고    scopus 로고
    • Mobile elements: Drivers of genome evolution
    • Kazazian, H. H. Jr. Mobile elements: drivers of genome evolution. Science 303, 1626-1632 (2004).
    • (2004) Science , vol.303 , pp. 1626-1632
    • Kazazian Jr., H.H.1
  • 2
    • 0003873979 scopus 로고    scopus 로고
    • Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. M. (eds) ASM Press, Washington DC
    • Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. M. (eds) Mobile DNA II (ASM Press, Washington DC, 2002).
    • (2002) Mobile DNA II
  • 3
    • 0034748934 scopus 로고    scopus 로고
    • Integron integrases possess a unique additional domain necessary for activity
    • Messier, N. & Roy, P. H. Integron integrases possess a unique additional domain necessary for activity. J. Bacteriol. 183, 6699-6706 (2001).
    • (2001) J. Bacteriol. , vol.183 , pp. 6699-6706
    • Messier, N.1    Roy, P.H.2
  • 4
    • 0041375463 scopus 로고    scopus 로고
    • New insight into site-specific recombination from Flp recombinase-DNA structures
    • Chen, Y. & Rice, P. A. New insight into site-specific recombination from Flp recombinase-DNA structures. Annu. Rev. Biophys. Biomol. Struct. 32, 135-159 (2003).
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 135-159
    • Chen, Y.1    Rice, P.A.2
  • 5
    • 0002627116 scopus 로고    scopus 로고
    • A structural view of tyrosine recombinase site-specific recombination
    • (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. M.) ASM Press, Washington DC
    • Van Duyne, G. A structural view of tyrosine recombinase site-specific recombination. In Mobile DNA II (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. M.) (ASM Press, Washington DC, 2002).
    • (2002) Mobile DNA II
    • Van Duyne, G.1
  • 6
    • 0001931646 scopus 로고    scopus 로고
    • Lambda integrase and the lambda Int family
    • (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. M.) ASM Press, Washington DC
    • Azaro, M. A. & Landy, A. Lambda integrase and the lambda Int family. In Mobile DNA II (eds Craig, N. L., Craigie, R., Gellert, M. & Lambowitz, A. M.) (ASM Press, Washington DC, 2002).
    • (2002) Mobile DNA II
    • Azaro, M.A.1    Landy, A.2
  • 7
    • 0030698334 scopus 로고    scopus 로고
    • Structure and function of 59-base element recombination sites associated with mobile gene cassettes
    • Stokes, H. W., O'Gorman, D. B., Recchia, G. D., Parsekhian, M. & Hall, R. M. Structure and function of 59-base element recombination sites associated with mobile gene cassettes. Mol. Microbiol. 26, 731-745 (1997).
    • (1997) Mol. Microbiol. , vol.26 , pp. 731-745
    • Stokes, H.W.1    O'Gorman, D.B.2    Recchia, G.D.3    Parsekhian, M.4    Hall, R.M.5
  • 8
    • 0032190242 scopus 로고    scopus 로고
    • DNA complexes obtained with the integron integrase Intl1 at the attI1 site
    • Gravel, A., Fournier, B. & Roy, P. H. DNA complexes obtained with the integron integrase Intl1 at the attI1 site. Nucleic Acids Res. 26, 4347-4355 (1998).
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4347-4355
    • Gravel, A.1    Fournier, B.2    Roy, P.H.3
  • 9
    • 0024454281 scopus 로고
    • Site-specific recombination by Tn3 resolvase
    • Stark, W. M., Boocock, M. R. & Sherratt, D. J. Site-specific recombination by Tn3 resolvase. Trends Genet 5, 304-309 (1989).
    • (1989) Trends Genet , vol.5 , pp. 304-309
    • Stark, W.M.1    Boocock, M.R.2    Sherratt, D.J.3
  • 10
    • 0030886293 scopus 로고    scopus 로고
    • Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse
    • Guo, F., Gopaul, D. N. & van Duyne, G. D. Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Nature 389, 40-46 (1997).
    • (1997) Nature , vol.389 , pp. 40-46
    • Guo, F.1    Gopaul, D.N.2    Van Duyne, G.D.3
  • 11
    • 0030700665 scopus 로고    scopus 로고
    • Non-palindromic attI sites of integrons are capable of site-specific recombination with one another and with secondary targets
    • Hansson, K., Skold, O. & Sundstrom, L. Non-palindromic attI sites of integrons are capable of site-specific recombination with one another and with secondary targets. Mol. Microbiol. 26, 441-453 (1997).
    • (1997) Mol. Microbiol. , vol.26 , pp. 441-453
    • Hansson, K.1    Skold, O.2    Sundstrom, L.3
  • 12
    • 29244454620 scopus 로고    scopus 로고
    • Integron cassette insertion: A recombination process involving a folded single strand substrate
    • Bouvier, M., Demarre, G. & Mazel, D. Integron cassette insertion: a recombination process involving a folded single strand substrate. EMBO J. 24, 4356-4367 (2005).
    • (2005) EMBO J. , vol.24 , pp. 4356-4367
    • Bouvier, M.1    Demarre, G.2    Mazel, D.3
  • 13
    • 14244267061 scopus 로고    scopus 로고
    • Comparative study of class 1 integron and Vibrio cholerae superintegron integrase activities
    • Biskri, L., Bouvier, M., Guerout, A. M., Boisnard, S. & Mazel, D. Comparative study of class 1 integron and Vibrio cholerae superintegron integrase activities. J. Bacteriol. 187, 1740-1750 (2005).
    • (2005) J. Bacteriol. , vol.187 , pp. 1740-1750
    • Biskri, L.1    Bouvier, M.2    Guerout, A.M.3    Boisnard, S.4    Mazel, D.5
  • 14
    • 0037350819 scopus 로고    scopus 로고
    • Comparative analysis of superintegrons: Engineering extensive genetic diversity in the Vibrionaceae
    • Rowe-Magnus, D. A., Guerout, A. M., Biskri, L., Bouige, P. & Mazel, D. Comparative analysis of superintegrons: engineering extensive genetic diversity in the Vibrionaceae. Genome Res. 13, 428-442 (2003).
    • (2003) Genome Res. , vol.13 , pp. 428-442
    • Rowe-Magnus, D.A.1    Guerout, A.M.2    Biskri, L.3    Bouige, P.4    Mazel, D.5
  • 16
    • 0032730443 scopus 로고    scopus 로고
    • The Intl1 integron integrase preferentially binds single-stranded DNA of the attC site
    • Francia, M. V., Zabala, J. C., de la Cruz, F. & Garcia Lobo, J. M. The Intl1 integron integrase preferentially binds single-stranded DNA of the attC site. J. Bacteriol. 181, 6844-6849 (1999).
    • (1999) J. Bacteriol. , vol.181 , pp. 6844-6849
    • Francia, M.V.1    Zabala, J.C.2    De La Cruz, F.3    Garcia Lobo, J.M.4
  • 17
    • 0032562596 scopus 로고    scopus 로고
    • A distinctive class of integron in the Vibrio cholerae genome
    • Mazel, D., Dychinco, B., Webb, V. A. & Davies, J. A distinctive class of integron in the Vibrio cholerae genome. Science 280, 605-608 (1998).
    • (1998) Science , vol.280 , pp. 605-608
    • Mazel, D.1    Dychinco, B.2    Webb, V.A.3    Davies, J.4
  • 18
    • 0030817595 scopus 로고    scopus 로고
    • Crystal structure of the site-specific recombinase, XerD
    • Subramanya, H. S. et al. Crystal structure of the site-specific recombinase, XerD. EMBO J. 16, 5178-5187 (1997).
    • (1997) EMBO J. , vol.16 , pp. 5178-5187
    • Subramanya, H.S.1
  • 19
    • 0043127393 scopus 로고    scopus 로고
    • A conformational switch controls the DNA cleavage activity of λ integrase
    • Aihara, H., Kwon, H. J., Nunes-Duby, S. E., Landy, A. & Ellenberger, T. A conformational switch controls the DNA cleavage activity of λ integrase. Mol. Cell 12, 187-198 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 187-198
    • Aihara, H.1    Kwon, H.J.2    Nunes-Duby, S.E.3    Landy, A.4    Ellenberger, T.5
  • 20
    • 0033637213 scopus 로고    scopus 로고
    • Crystal structure of a Flp recombinase-Holliday junction complex: Assembly of an active oligomer by helix swapping
    • Chen, Y., Narendra, U., Iype, L. E., Cox, M. M. & Rice, P. A. Crystal structure of a Flp recombinase-Holliday junction complex: assembly of an active oligomer by helix swapping. Mol. Cell 6, 885-897 (2000).
    • (2000) Mol. Cell , vol.6 , pp. 885-897
    • Chen, Y.1    Narendra, U.2    Iype, L.E.3    Cox, M.M.4    Rice, P.A.5
  • 21
    • 0001656001 scopus 로고    scopus 로고
    • Flexibility in DNA recombination: Structure of the lambda integrase catalytic core
    • Kwon, H. J., Tirumalai, R., Landy, A. & Ellenberger, T. Flexibility in DNA recombination: structure of the lambda integrase catalytic core. Science 276, 126-131 (1997).
    • (1997) Science , vol.276 , pp. 126-131
    • Kwon, H.J.1    Tirumalai, R.2    Landy, A.3    Ellenberger, T.4
  • 22
    • 0030904786 scopus 로고    scopus 로고
    • Molecular organization in site-specific recombination: The catalytic domain of bacteriophage HP1 integrase at 2.7 Å resolution
    • Hickman, A. B., Waninger, S., Scocca, J. J. & Dyda, F. Molecular organization in site-specific recombination: the catalytic domain of bacteriophage HP1 integrase at 2.7 Å resolution. Cell 89, 227-237 (1997).
    • (1997) Cell , vol.89 , pp. 227-237
    • Hickman, A.B.1    Waninger, S.2    Scocca, J.J.3    Dyda, F.4
  • 23
    • 0033634688 scopus 로고    scopus 로고
    • Catalytic mechanism of DNA topoisomerase IB
    • Krogh, B. O. & Shuman, S. Catalytic mechanism of DNA topoisomerase IB. Mol. Cell 5, 1035-1041 (2000).
    • (2000) Mol. Cell , vol.5 , pp. 1035-1041
    • Krogh, B.O.1    Shuman, S.2
  • 24
    • 0029806695 scopus 로고    scopus 로고
    • Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction
    • Rafferty, J. B. et al. Crystal structure of DNA recombination protein RuvA and a model for its binding to the Holliday junction. Science 274, 415-421 (1996).
    • (1996) Science , vol.274 , pp. 415-421
    • Rafferty, J.B.1
  • 25
    • 0032821668 scopus 로고    scopus 로고
    • Structure and mechanism in site-specific recombination
    • Gopaul, D. N. & Van Duyne, G. D. Structure and mechanism in site-specific recombination. Curr. Opin. Struct. Biol. 9, 14-20 (1999).
    • (1999) Curr. Opin. Struct. Biol. , vol.9 , pp. 14-20
    • Gopaul, D.N.1    Van Duyne, G.D.2
  • 26
    • 0030927777 scopus 로고    scopus 로고
    • Action of site-specific recombinases XerC and XerD on tethered Holliday junctions
    • Arciszewska, L. K., Grainge, I. & Sherratt, D. J. Action of site-specific recombinases XerC and XerD on tethered Holliday junctions. EMBO J. 16, 3731-3743 (1997).
    • (1997) EMBO J. , vol.16 , pp. 3731-3743
    • Arciszewska, L.K.1    Grainge, I.2    Sherratt, D.J.3
  • 27
    • 21344466779 scopus 로고    scopus 로고
    • A structural basis for allosteric control of DNA recombination by λ integrase
    • Biswas, T. et al. A structural basis for allosteric control of DNA recombination by λ integrase. Nature 435, 1059-1066 (2005).
    • (2005) Nature , vol.435 , pp. 1059-1066
    • Biswas, T.1
  • 28
    • 0029240229 scopus 로고
    • Swapping DNA strands and sensing homology without branch migration in λ site-specific recombination
    • Nunes-Duby, S. E., Azaro, M. A. & Landy, A. Swapping DNA strands and sensing homology without branch migration in λ site-specific recombination. Curr. Biol. 5, 139-148 (1995).
    • (1995) Curr. Biol. , vol.5 , pp. 139-148
    • Nunes-Duby, S.E.1    Azaro, M.A.2    Landy, A.3
  • 29
    • 0032528271 scopus 로고    scopus 로고
    • Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination
    • Gopaul, D. N., Guo, F. & Van Duyne, G. D. Structure of the Holliday junction intermediate in Cre-loxP site-specific recombination. EMBO J. 17, 4175-4187 (1998).
    • (1998) EMBO J. , vol.17 , pp. 4175-4187
    • Gopaul, D.N.1    Guo, F.2    Van Duyne, G.D.3
  • 30
    • 0025098475 scopus 로고
    • Characterization of Holliday structures in FLP protein-promoted site-specific recombination
    • Meyer-Leon, L., Inman, R. B. & Cox, M. M. Characterization of Holliday structures in FLP protein-promoted site-specific recombination. Mol. Cell. Biol. 10, 235-242 (1990).
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 235-242
    • Meyer-Leon, L.1    Inman, R.B.2    Cox, M.M.3
  • 31
    • 0034682335 scopus 로고    scopus 로고
    • Lateral gene transfer and the nature of bacterial innovation
    • Ochman, H., Lawrence, J. G. & Groisman, E. A. Lateral gene transfer and the nature of bacterial innovation. Nature 405, 299-304 (2000).
    • (2000) Nature , vol.405 , pp. 299-304
    • Ochman, H.1    Lawrence, J.G.2    Groisman, E.A.3
  • 32
    • 0028010888 scopus 로고
    • Hhal methyltransferase flips its target base out of the DNA helix
    • Klimasauskas, S., Kumar, S., Roberts, R. J. & Cheng, X. Hhal methyltransferase flips its target base out of the DNA helix. Cell 76, 357-369 (1994).
    • (1994) Cell , vol.76 , pp. 357-369
    • Klimasauskas, S.1    Kumar, S.2    Roberts, R.J.3    Cheng, X.4
  • 33
    • 23744489154 scopus 로고    scopus 로고
    • The single-stranded genome of phage CTX is the form used for integration into the genome of Vibrio choleras
    • Val, M. E. et al. The single-stranded genome of phage CTX is the form used for integration into the genome of Vibrio choleras. Mol. Cell 19, 559-566 (2005).
    • (2005) Mol. Cell , vol.19 , pp. 559-566
    • Val, M.E.1
  • 34
    • 25844521203 scopus 로고    scopus 로고
    • Active site sharing and subterminal hairpin recognition in a new class of DNA transposases
    • Running, D. R. et al. Active site sharing and subterminal hairpin recognition in a new class of DNA transposases. Mol. Cell 20, 143-154 (2005).
    • (2005) Mol. Cell , vol.20 , pp. 143-154
    • Running, D.R.1
  • 35
    • 0036047412 scopus 로고    scopus 로고
    • Bacterial conjugation: A two-step mechanism for DNA transport
    • Llosa, M., Gomis-Ruth, F. X., Coll, M. & de la Cruz, F. Bacterial conjugation: a two-step mechanism for DNA transport. Mol. Microbiol. 45, 1-8 (2002).
    • (2002) Mol. Microbiol. , vol.45 , pp. 1-8
    • Llosa, M.1    Gomis-Ruth, F.X.2    Coll, M.3    De La Cruz, F.4
  • 36
    • 0027879008 scopus 로고
    • Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants
    • Kabsch, W. Automatic processing of rotation diffraction data from crystals of initially unknown symmetry and cell constants. J. Appl. Cryst. 26, 795-800 (1993).
    • (1993) J. Appl. Cryst. , vol.26 , pp. 795-800
    • Kabsch, W.1
  • 37
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D , vol.50 , pp. 760-763
  • 38
    • 0042810719 scopus 로고    scopus 로고
    • Towards automated protein structure determination: BnP, the SnB-PHASES interface
    • Weeks, C. M. et al. Towards automated protein structure determination: BnP, the SnB-PHASES interface. Z. Kristallogr. 217, 686-693 (2002).
    • (2002) Z. Kristallogr. , vol.217 , pp. 686-693
    • Weeks, C.M.1
  • 39
    • 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, 110-119 (1991).
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 40
    • 3543012707 scopus 로고    scopus 로고
    • Crystallography & NMR system: A new software suite for macromolecular structure determination
    • Brunger, A. T. et al. Crystallography & NMR system: a new software suite for macromolecular structure determination. Acta Crystallogr. D 54, 905-921 (1998).
    • (1998) Acta Crystallogr. D , vol.54 , pp. 905-921
    • Brunger, A.T.1


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