A versatile and efficient high-throughput cloning tool for structural biology.

Methods for the cloning of large numbers of open reading frames into expression vectors are of critical importance for challenging structural biology projects. Here we describe a system termed fragment exchange (FX) cloning that facilitates the high-throughput generation of expression constructs. The method is based on a class IIS restriction enzyme and negative selection markers. FX cloning combines attractive features of established recombination- and ligation-independent cloning methods: It allows the straightforward transfer of an open reading frame into a variety of expression vectors and is highly efficient and very economic in its use. In addition, FX cloning avoids the common but undesirable feature of significantly extending target open reading frames with cloning related sequences, as it leaves a minimal seam of only a single extra amino acid to either side of the protein. The method has proven to be very robust and suitable for all common pro- and eukaryotic expression systems. It considerably speeds up the generation of expression constructs compared to traditional methods and thus facilitates a broader expression screening.

[1]  S. Elledge,et al.  MAGIC, an in vivo genetic method for the rapid construction of recombinant DNA molecules , 2005, Nature Genetics.

[2]  Tobias Fromme,et al.  Rapid single step subcloning procedure by combined action of type II and type IIs endonucleases with ligase , 2007, Journal of biological engineering.

[3]  J. Hartley,et al.  DNA cloning using in vitro site-specific recombination. , 2000, Genome research.

[4]  D. Rees,et al.  The funnel approach to the precrystallization production of membrane proteins. , 2008, Journal of molecular biology.

[5]  F. Studier,et al.  Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. , 1986, Journal of molecular biology.

[6]  W. D. de Vos,et al.  Characterization of the nisin gene cluster nisABTCIPR of Lactococcus lactis. Requirement of expression of the nisA and nisI genes for development of immunity. , 1993, European journal of biochemistry.

[7]  E. Salah,et al.  High throughput production of recombinant human proteins for crystallography. , 2008, Methods in molecular biology.

[8]  S. Cohen,et al.  Analysis of gene control signals by DNA fusion and cloning in Escherichia coli. , 1980, Journal of molecular biology.

[9]  T. Nagai,et al.  A high-throughput and single-tube recombination of crude PCR products using a DNA polymerase inhibitor and type IIS restriction enzyme. , 2008, Journal of biotechnology.

[10]  W. D. de Vos,et al.  Controlled gene expression systems for Lactococcus lactis with the food-grade inducer nisin , 1996, Applied and environmental microbiology.

[11]  K. Gunsalus,et al.  Protein production and purification , 2008, Nature Methods.

[12]  M. Couturier,et al.  Positive-selection vectors using the F plasmid ccdB killer gene. , 1994, Gene.

[13]  Eric Gouaux,et al.  Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. , 2006, Structure.

[14]  W. Sandine,et al.  Improved Medium for Lactic Streptococci and Their Bacteriophages , 1975, Applied microbiology.

[15]  Marco Punta,et al.  The New York Consortium on Membrane Protein Structure (NYCOMPS): a high-throughput platform for structural genomics of integral membrane proteins , 2010, Journal of Structural and Functional Genomics.

[16]  W. Szybalski,et al.  ErratumClass-IIS restriction enzymes- a review , 1991 .

[17]  Nick S Berrow,et al.  The precise engineering of expression vectors using high-throughput In-Fusion PCR cloning. , 2009, Methods in molecular biology.

[18]  D. Belin,et al.  Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter , 1995, Journal of bacteriology.

[19]  B. Poolman,et al.  High-throughput cloning and expression in recalcitrant bacteria , 2007, Nature Methods.

[20]  Carola Engler,et al.  A One Pot, One Step, Precision Cloning Method with High Throughput Capability , 2008, PloS one.

[21]  Tony Pawson,et al.  Modification of the Creator recombination system for proteomics applications – improved expression by addition of splice sites , 2006, BMC biotechnology.

[22]  J. Sorge,et al.  Creating seamless junctions independent of restriction sites in PCR cloning. , 1996, Gene.

[23]  R. Dutzler,et al.  X-ray structure of the C-terminal domain of a prokaryotic cation-chloride cotransporter. , 2009, Structure.

[24]  Eric R Geertsma,et al.  Quality control of overexpressed membrane proteins , 2008, Proceedings of the National Academy of Sciences.

[25]  P. D. de Jong,et al.  Coincidence cloning of Alu PCR products. , 1991, Proceedings of the National Academy of Sciences of the United States of America.

[26]  B. Poolman,et al.  Production of membrane proteins in Escherichia coli and Lactococcus lactis. , 2010, Methods in molecular biology.

[27]  J. Hartley,et al.  Cloning technologies for protein expression and purification. , 2006, Current opinion in biotechnology.

[28]  C. Robert,et al.  Conditional suicide system of Escherichia coli released into soil that uses the Bacillus subtilis sacB gene , 1993, Applied and environmental microbiology.

[29]  S. Lesley Parallel methods for expression and purification. , 2009, Methods in enzymology.

[30]  J. Heitman,et al.  A nomenclature for restriction enzymes, DNA methyltransferases, homing endonucleases and their genes. , 2003, Nucleic acids research.

[31]  G. Gamba Molecular physiology and pathophysiology of electroneutral cation-chloride cotransporters. , 2005, Physiological reviews.