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Because the DNA segments are cut and reorganized in a direction-specific manner, site-specific recombination has emerged as an efficient genetic engineering technique. Flippase and Cyclization recombinases or Flp and Cre, respectively, are two members of the tyrosine recombinase family derived from bacteriophages, that are used to mediate site-specific DNA insertions, deletions, and targeted expression of proteins in mammalian cell lines.
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Cells are sometimes infected by more than one virus at once. When two viruses disassemble to expose their genomes for replication in the same cell, similar regions of their genomes can pair together and exchange sequences in a process called recombination. Alternatively, viruses with segmented genomes can swap segments in a process called reassortment.
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Reproductive cloning is the process of producing a genetically identical copy—a clone—of an entire organism. While clones can be produced by splitting an early embryo—similar to what happens naturally with identical twins—cloning of adult animals is usually done by a process called somatic cell nuclear transfer (SCNT).
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Recombinational cloning.

Jaehong Park1, Joshua Labaer

  • 1Harvard Medical School, Cambridge, Massachusetts, USA.

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Summary
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Functional proteomics requires full-length cDNAs in expression vectors. Recombinational cloning offers a rapid, efficient method for transferring DNA inserts into multiple expression systems, simplifying protein analysis.

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Area of Science:

  • Molecular Biology
  • Protein Expression
  • Functional Proteomics

Background:

  • Functional proteomics relies on the availability of full-length complementary DNAs (cDNAs) within expression-ready plasmid vectors.
  • Efficiently generating these expression-ready clones is crucial for subsequent protein expression and functional analysis.
  • Classical restriction enzyme-based cloning methods can be time-consuming and less efficient for parallel cloning tasks.

Purpose of the Study:

  • To summarize strategies for generating expression-ready clones using recombinational cloning technologies.
  • To highlight the advantages of recombinational cloning for functional proteomics research.
  • To introduce two popular commercial recombinational cloning systems: Invitrogen's Gateway and BD Clontech's Creator.

Main Methods:

  • Utilizing site-specific recombination, a universal cloning technique independent of the insert DNA sequence.
  • Employing recombinational cloning for rapid and efficient parallel transfer of DNA inserts.
  • Summarizing established strategies for generating expression-ready clones with commercial kits.

Main Results:

  • Recombinational cloning provides a universal and efficient method for cloning DNA inserts.
  • This technique facilitates the rapid parallel transfer of DNA into multiple expression systems.
  • Commercial systems like Gateway and Creator streamline the generation of expression-ready clones.

Conclusions:

  • Recombinational cloning significantly enhances the workflow for functional proteomics by simplifying clone generation.
  • The described strategies enable efficient protein expression and functional analysis through readily available expression-ready clones.
  • Adoption of these recombinational cloning technologies can accelerate research in protein science.