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Microbiology and Molecular Biology Reviews, June 2009, p. 300-309, Vol. 73, No. 2
1092-2172/09/$08.00+0     doi:10.1128/MMBR.00038-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Challenging a Paradigm: the Role of DNA Homology in Tyrosine Recombinase Reactions

Lara Rajeev,1* Karolina Malanowska,2 and Jeffrey F. Gardner2

Department of Civil and Environmental Engineering, University of Washington, Seattle, Washington,1 Department of Microbiology, University of Illinois at Urbana—Champaign, Champaign, Illinois2

Summary: A classical feature of the tyrosine recombinase family of proteins catalyzing site-specific recombination, as exemplified by the phage lambda integrase and the Cre and Flp recombinases, is the ability to recombine substrates sharing very limited DNA sequence identity. Decades of research have established the importance of this short stretch of identity within the core regions of the substrates. Since then, several new enzymes that challenge this paradigm have been discovered and require the role of sequence identity in site-specific recombination to be reconsidered. The integrases of the conjugative transposons such as Tn916, Tn1545, and CTnDOT recombine substrates with heterologous core sequences. The integrase of the mobilizable transposon NBU1 performs recombination more efficiently with certain core mismatches. The integration of CTX phage and capture of gene cassettes by integrons also occur by altered mechanisms. In these systems, recombination occurs between mismatched sequences by a single strand exchange. In this review, we discuss literature that led to the formulation of the current strand-swapping isomerization model for tyrosine recombinases. The review then focuses on recent developments on the recombinases that challenged the paradigm that was derived from the studies of early systems.

* Corresponding author. Mailing address: Department of Civil and Environmental Engineering, University of Washington, 616 NE Northlake Place, Rm. 476D, Seattle, WA 98125. Phone: (206) 543 5454. Fax: (206) 616-5721. E-mail: lrajeev{at}u.washington.edu

Microbiology and Molecular Biology Reviews, June 2009, p. 300-309, Vol. 73, No. 2
1092-2172/09/$08.00+0     doi:10.1128/MMBR.00038-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Frumerie, C., Ducos-Galand, M., Gopaul, D. N., Mazel, D. (2009). The relaxed requirements of the integron cleavage site allow predictable changes in integron target specificity. Nucleic Acids Res 0: gkp990v1-gkp990 [Abstract] [Full Text]  


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