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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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Detection of Homologous Recombination Intermediates via Proximity Ligation and Quantitative PCR in Saccharomyces cerevisiae
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Irreversible sortase A-mediated ligation driven by diketopiperazine formation.

Fa Liu1, Ethan Y Luo, David B Flora

  • 1Lilly Research Laboratories , Indianapolis, Indiana 46285, United States.

The Journal of Organic Chemistry
|January 1, 2014
PubMed
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Sortase A (SrtA) ligation is useful but reversible. New SrtA substrates form diketopiperazines, enabling irreversible ligation and overcoming efficiency limitations in bioorganic chemistry.

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Area of Science:

  • Bioorganic chemistry
  • Biochemistry
  • Synthetic chemistry

Background:

  • Sortase A (SrtA)-mediated ligation offers high specificity under physiological conditions.
  • The reversible nature of SrtA ligation limits its efficiency and broad application.
  • Overcoming reversibility is key to advancing SrtA ligation techniques.

Purpose of the Study:

  • To develop novel Sortase A (SrtA) substrates for irreversible ligation.
  • To enhance the efficiency and utility of SrtA-mediated bioconjugation.
  • To address the limitations posed by the reversible nature of SrtA ligation.

Main Methods:

  • Design and synthesis of novel SrtA substrates: LPETGG-isoacyl-Ser and LPETGG-isoacyl-Hse.
  • Utilizing diketopiperazine (DKP) formation to irreversibly trap SrtA-excised peptide fragments.
  • Testing ligation efficiency with N-terminal Gly-containing moieties.

Main Results:

  • Successful irreversible ligation of novel SrtA substrates to Gly-containing peptides.
  • Diketopiperazine (DKP) formation effectively deactivates the SrtA-excised fragment.
  • The new substrates demonstrate stability in ligation buffers.

Conclusions:

  • LPETGG-isoacyl-Ser and LPETGG-isoacyl-Hse are effective irreversible SrtA ligation substrates.
  • DKP formation provides a robust strategy for irreversible Sortase A ligation.
  • These novel substrates offer valuable alternatives for advancing bioorganic chemistry applications.