This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Parsons, R L Articles by Jayaram, M Search for Related Content PubMed PubMed Citation Articles by Parsons, R L Articles by Jayaram, M

 Previous Article  |  Next Article 

Mol Cell Biol. 1988 August; 8(8): 3303-3310

Step-arrest mutants of FLP recombinase: implications for the catalytic mechanism of DNA recombination.

Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, California 92037.

ABSTRACT

The site-specific recombinase (FLP) encoded by the yeast plasmid 2 micron circle belongs to the integrase (of phage lambda) family of recombinases. The sparse homology within the members of this family contrasts with the invariance of three residues, His-396, Arg-399, and Tyr-433 (the numbers correspond to the family alignment positions), among them. We report here results on substrate recognition and catalysis by FLP proteins altered at these residues. Mutations of the conserved His and Tyr that aborted the reaction at specific steps of catalysis permitted genetic dissection of the possible biochemical steps of recombination. We provide indirect evidence that recombination by FLP proceeds through a Holliday junction intermediate.

This article has been cited by other articles:

• Bryan, A., Roesch, P., Davis, L., Moritz, R., Pellett, S., Welch, R. A. (2006). Regulation of Type 1 Fimbriae by Unlinked FimB- and FimE-Like Recombinases in Uropathogenic Escherichia coli Strain CFT073. Infect. Immun. 74: 1072-1083 [Abstract] [Full Text]  
• Xu, C.-J., Ahn, Y.-T., Pathania, S., Jayaram, M. (1998). Flp Ribonuclease Activities. MECHANISTIC SIMILARITIES AND CONTRASTS TO SITE-SPECIFIC DNA RECOMBINATION. J. Biol. Chem. 273: 30591-30598 [Abstract] [Full Text]  
• Knudsen, B. R., Lee, J., Lisby, M., Westergaard, O., Jayaram, M. (1998). Alcoholysis and Strand Joining by the Flp Site-specific Recombinase. MECHANISTICALLY EQUIVALENT REACTIONS MEDIATED BY DISTINCT CATALYTIC CONFIGURATIONS. J. Biol. Chem. 273: 22028-22036 [Abstract] [Full Text]  
• Lee, J., Tonozuka, T., Jayaram, M. (1997). Mechanism of active site exclusion in a site-specific recombinase: role of the DNA substrate in conferring half-of-the-sites activity. Genes Dev. 11: 3061-3071 [Abstract] [Full Text]  
• Cornet, F., Hallet, B., Sherratt, D. J. (1997). Xer Recombination in Escherichia coli. SITE-SPECIFIC DNA TOPOISOMERASE ACTIVITY OF THE XerC and XerD RECOMBINASES. J. Biol. Chem. 272: 21927-21931 [Abstract] [Full Text]  
• Zhu, X.-D., Sadowski, P. D. (1995). Cleavage-dependent Ligation by the FLP Recombinase. J. Biol. Chem. 270: 23044-23054 [Abstract] [Full Text]  
• Lee, J., Jayaram, M. (1995). Functional Roles of Individual Recombinase Monomers in Strand Breakage and Strand Union during Site-specific DNA Recombination. J. Biol. Chem. 270: 23203-23211 [Abstract] [Full Text]  
• Kim, K., Namgoong, S.-Y., Jayaram, M., Harshey, R. M. (1995). Step-arrest Mutants of Phage Mu Transposase. J. Biol. Chem. 270: 1472-1479 [Abstract] [Full Text]  
• Krogh, B. O., Shuman, S. (2001). Vaccinia Topoisomerase Mutants Illuminate Conformational Changes during Closure of the Protein Clamp and Assembly of a Functional Active Site. J. Biol. Chem. 276: 36091-36099 [Abstract] [Full Text]  
• Tribble, G., Ahn, Y.-T., Lee, J., Dandekar, T., Jayaram, M. (2000). DNA Recognition, Strand Selectivity, and Cleavage Mode during Integrase Family Site-specific Recombination. J. Biol. Chem. 275: 22255-22267 [Abstract] [Full Text]