NDLI: Directed evolution of the site specificity of Cre recombinase

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Directed evolution of the site specificity of Cre recombinase

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Schultz, Peter G. Santoro, Stephen W.
Description	Author Affiliation: Santoro SW ( Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, SR202, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.);
Abstract	Cre recombinase from bacteriophage P1 recognizes a 34-bp recombination site, loxP, with exquisite sequence specificity and catalyzes the site-specific insertion, excision, or rearrangement of DNA. To better understand the molecular basis of protein-DNA recognition and generate recombinases with altered specificities, we have developed a directed evolution strategy that can be used to identify recombinases that recognize variant loxP sites. To be selected, members of a library of Cre variants produced by targeted random mutagenesis must rapidly catalyze recombination, in vivo, between two variant loxP sites that are located on a reporter plasmid. Recombination results in an altered pattern of fluorescent protein expression that can be identified by flow cytometry. Fluorescence-activated cell sorting can be used either to screen positively for recombinase variants that recognize a novel loxP site, or negatively for variants that cannot recognize the wild-type loxP site. The use of positive screening alone resulted in a relaxation of recombination site specificity, whereas a combination of positive and negative screening resulted in a switching of specificity. One of the identified recombinases selectively recombines a novel recombination site and operates at a rate identical to that of wild-type Cre. Analysis of the sequences of the resulting Cre variants provides insight into the evolution of these altered specificities. This and other systems should contribute to our understanding of protein-DNA recognition and may eventually be used to evolve custom-tailored recombinases that can be used for gene study and inactivation.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	7
Volume Number	99
Language	English
Publisher	National Academy of Sciences
Publisher Date	2002-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Integrases Genetics Recombination, Genetic Viral Proteins Amino Acid Sequence Biological Evolution Gene Library Chemistry Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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