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Cross-talk between diverse serine integrases.

Shweta Singh1, Kate Rockenbach1, Rebekah M Dedrick1

  • 1Department of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15241, USA.

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|October 29, 2013
PubMed
Summary

Serine integrases are crucial for phage genome recombination. This study reveals unexpected cross-talk between two specific mycobacteriophage serine integrases, challenging their predictable use in synthetic biology.

Keywords:
BSAC-terminal domainCCCTDN-terminal domainNTDRDZDattachment site selectionbovine serum albumincoiled coilintegrasephage integrationrecombinase domainserine recombinasesite-specific recombinationzinc-nucleated domain

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Area of Science:

  • Molecular Biology
  • Genetics
  • Synthetic Biology

Background:

  • Phage-encoded serine integrases facilitate site-specific recombination of temperate phage genomes.
  • Their small attachment sites, lack of host factors, and directionality make them suitable for synthetic genetic circuits.
  • Independent function without cross-talk is desired for complex circuit construction.

Purpose of the Study:

  • To investigate the predictability and specificity of serine integrases in heterologous systems.
  • To characterize a pair of serine integrases from mycobacteriophages Bxz2 and Peaches with potentially unusual specificities.

Main Methods:

  • Comparative analysis of serine integrase sequences and their attP sites.
  • Investigation of recombination activity and specificity in a heterologous system.
  • Assessment of cross-talk between different serine integrase systems.

Main Results:

  • Two serine integrases from mycobacteriophages Bxz2 and Peaches exhibit unpredictable specificities.
  • Despite low sequence identity and distinct attP sites, these integrases share the same attB site.
  • Non-reciprocal cross-talk was observed between the Bxz2 and Peaches integrase systems.

Conclusions:

  • The DNA binding specificities are influenced by the configuration of half-sites within attachment site DNAs, not just specific DNA contacts.
  • The observed cross-talk challenges the assumption of independent function for these serine integrases in synthetic biology applications.
  • Further research is needed to fully understand and engineer serine integrase systems for reliable synthetic circuit design.