The influence of coiled-coil motif of serine recombinase toward the directionality regulation.

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  • Additional Information
    • Source:
      Publisher: Cell Press Country of Publication: United States NLM ID: 0370626 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1542-0086 (Electronic) Linking ISSN: 00063495 NLM ISO Abbreviation: Biophys J Subsets: MEDLINE
    • Publication Information:
      Publication: Cambridge, MA : Cell Press
      Original Publication: New York, Published by Rockefeller University Press [etc.] for the Biophysical Society.
    • Subject Terms:
      Recombinases*/genetics ; Bacteriophages*/genetics; Serine/metabolism ; Attachment Sites, Microbiological ; Recombination, Genetic ; Integrases/genetics ; Integrases/metabolism
    • Abstract:
      Serine integrases promote the recombination of two complementary DNA sequences, attP and attB, to create hybrid sequences, attL and attR. The reaction is unidirectional in the absence of an accessory protein called recombination directionality factor. We utilized tethered particle motion (TPM) experiments to investigate the reaction behaviors of two model serine integrases from Listeria innocua phage LI and Streptomyces coelicolor phage C31. Detailed kinetic analyses of wild-type and mutant proteins were carried out to verify the mechanisms of recombination directionality. In particular, we assessed the influence of a coiled-coil motif (CC) that is conserved in the C-terminal domain of serine integrases and is an important prerequisite for efficient recombination. Compared to wild type, we found that CC deletions in both serine integrases reduced the overall abundance of integrase (Int) att-site complexes and favored the formation of nonproductive complexes over recombination-competent complexes. Furthermore, the rate at which CC mutants formed productive synaptic complexes and disassembled aberrant nonproductive complexes was significantly reduced. It is notable that while the φC31 Int CC is essential for recombination, the LI Int CC plays an auxiliary role for recombination to stabilize protein-protein interactions and to control the directionality of the reaction.
      Competing Interests: Declaration of interests The authors declare no competing interests.
      (Copyright © 2023 Biophysical Society. Published by Elsevier Inc. All rights reserved.)
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    • Grant Information:
      United Kingdom WT_ Wellcome Trust
    • Accession Number:
      0 (Recombinases)
      452VLY9402 (Serine)
      EC 2.7.7.- (Integrases)
    • Publication Date:
      Date Created: 20231117 Date Completed: 20231222 Latest Revision: 20240331
    • Publication Date:
      20240401
    • Accession Number:
      PMC10754689
    • Accession Number:
      10.1016/j.bpj.2023.11.009
    • Accession Number:
      37974397