Mechanism of Cleavage and Ligation by FLP Recombinase: Classification of Mutations in FLP Protein by in Vitro Complementation Analysis

REFERENCES

• Abremski, K. E., and R. H. Hoess. 1992. Evidence for a second conserved arginine residue in the integrase family of recombination proteins. Protein Eng. 5:87–91.
   PubMedGoogle Scholar
• Amin, A., H. Roca, K. Luetke, and P. D. Sadowski. 1991. Synapsis, strand scission, and strand exchange induced by the FLP recombinase: analysis with half-FRT sites. Mol. Cell. Biol. 11:4497–4508.
   PubMedGoogle Scholar
• Andrews, B. J., L. G. Beatty, and P. D. Sadowski. 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.
   PubMedGoogle Scholar
• Andrews, B. J., G. A. Protean, L. G. Beatty, and P. D. Sadowski. 1985. The FLP recombinase of the 2 μ circle DNA of yeast: interaction with its target sequences. Cell 40:795–803.
   PubMedGoogle Scholar
• Argos, P., A. Landy, K. Abremski, J. B. Egan, E. H. Ljunguist, R. H. Hoess, M. L. Kahn, S. V. L Manayana, L. S. Pierson III, N. Sternberg, and J. M. Leong. 1986. The integrase family of site-specific recombinases: regional similarities and global diversity. EMBO J. 5:433–440.
   PubMed Web of Science ®Google Scholar
• Bruckner, R. C., and M. M. Cox. 1986. Specific-contacts between the FLP protein of the yeast 2 micron plasmid and its recombination site. J. Biol. Chem. 261:11798–11807.
   PubMed Web of Science ®Google Scholar
• Chen, J.-W., J. Lee, and M. Jayaram. 1992. DNA-cleavage in trans by the active tyrosine during FLP recombination: switching protein partners before exchanging strands. Cell 69:647–658.
   PubMedGoogle Scholar
• Cox, M. M. 1989. DNA inversion in the 2 μm plasmid of Saccharomyces cerevisiae, p. 661–670. In D. E. Berg and M. M. Howe (ed.), Mobile DNA. American Society for Microbiology, Washington, D.C.
   Google Scholar
• Dixon, J. Unpublished data.
   Google Scholar
• Evans, B., J.-W. Chen, R. L. Parsons, T. K. Bauer, D. B. Teplow, and M. Jayaram. 1990. Identification of the active site tyrosine of FLP recombinase: possible relevance to the mechanism of recombination. J. Biol. Chem. 265:18504–18510.
   PubMedGoogle Scholar
• Friesen, H. Unpublished data.
   Google Scholar
• Friesen, H., and P. D. Sadowski. 1992. Mutagenesis of a conserved region of the gene encoding the FLP recombinase of Saccharomyces cerevisiae. A role for arginine 191 in binding and ligation. J. Mol. Biol. 225:313–326.
   PubMedGoogle Scholar
• Jayaram, M., K. L. Crain, R. L. Parsons, and R. M. Harshey. 1988. Holliday junctions in FLP recombination. Resolution by step-arrest mutants of FLP protein. Proc. Natl. Acad. Sci. USA 85:7902–7906.
   PubMedGoogle Scholar
• Kulpa, J., J. E. Dixon, G. Pan, and P. D. Sadowski. 1993. Mutations of FLP recombinase gene that cause a deficiency in DNA bending and strand cleavage. J. Biol. Chem. 268:1101–1108.
   PubMedGoogle Scholar
• Luetke, K. Unpublished data.
   Google Scholar
• Pan, G., K. Luetke, C. D. Juby, R. Brousseau, and P. D. Sadowski. 1993. Ligation of synthetic activated DNA substrates by site-specific recombinases. J. Biol. Chem. 268:3683–3689.
   PubMedGoogle Scholar
• Pan, G., and P. D. Sadowski. 1992. Ligation activity of FLP recombinase. The strand ligation activity of a site-specific recombinase using an activated DNA substrate. J. Biol. Chem. 267:12397–12399.
   PubMedGoogle Scholar
• Parsons, R. L., B. R. Evans, L. Zheng, and M. Jayaram. 1990. Functional analysis of Arg-308 mutants of FLP recombinase. J. Biol. Chem. 265:4527–4533.
   PubMedGoogle Scholar
• Parsons, R. L., P. V. Prasad, R. M. Harshey, and M. Jayaram. 1988. Step-arrest mutants of FLP recombinase: implications for the catalytic mechanism of DNA recombination. Mol. Cell. Biol. 8:3303–3310.
   PubMed Web of Science ®Google Scholar
• Prasad, P. V., L.-S. Young, and M. Jayaram. 1987. Mutations in the 2μm circle site-specific recombinase that abolish recombination without affecting substrate recognition. Proc. Natl. Acad. Sci. USA 74:5463–5467.
   Google Scholar
• Qian, X.-H·, R. B. Inman, and M. M. Cox. 1990. Protein-based asymmetry and protein-protein interactions in FLP recombinase-mediated site specific recombination. J. Biol. Chem. 265:21779–21788.
   PubMedGoogle Scholar
• Schwartz, C. J. E., and P. D. Sadowski. 1989. FLP recombinase of the 2 μM circle plasmid of Saccharomyces cerevisiae bends its DNA target. Isolation of FLP mutants defective in DNA bending. J. Mol. Biol. 205:647–658.
   PubMed Web of Science ®Google Scholar
• Schwartz, C. J. E., and P. D. Sadowski. 1990. The FLP protein of the 2-micron circle plasmid of yeast induces multiple bends in the FLP recognition target site. J. Mol. Biol. 216:289–298.
   PubMedGoogle Scholar
• Shaikh, A., and J. E. Dixon. Unpublished data.
   Google Scholar
• Utatsu, I., S. Sukamoto, T. Imura, and A. Toh-E. 1987. Yeast plasmids resembling 2 μm DNA: regional similarities and diversities at the molecular level. J. Bacteriol. 169:5537–5545.
   PubMedGoogle Scholar