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TitleStructural basis of directionality control in large serine integrases.
Journal, issue, pagesbioRxiv, Year 2025
Publish dateJan 13, 2025
AuthorsHeewhan Shin / Ying Pigli / Tania Peña Reyes / James R Fuller / Femi J Olorunniji / Phoebe A Rice /
PubMed AbstractLarge serine integrases (LSIs) catalyze unidirectional site-specific DNA recombination reactions, yet those reactions are reversed by the presence of a cognate recombination directionality factor ...Large serine integrases (LSIs) catalyze unidirectional site-specific DNA recombination reactions, yet those reactions are reversed by the presence of a cognate recombination directionality factor (RDF). Mechanistic understanding of directionality control has been hampered by a lack of structural information. Here, we use cryo-electron microscopy (cryo-EM) to determine the structures of six SPbeta integrase-DNA complexes along the integrative (-RDF) and excisive (+RDF) reaction pathways, at 4.16-7.18Å resolution. Our findings reveal how RDF-mediated repositioning of an integrase subdomain (1) dictates which pairs of DNA sites can be assembled into a synaptic complex to initiate recombination and (2) dictates which product complexes will be conformationally locked, preventing the back reaction. These mechanistic insights provide a conceptual framework for engineering efficient and versatile genome editing tools.
External linksbioRxiv / PubMed:39803483 / PubMed Central
MethodsEM (single particle)
Resolution3.31 - 7.1 Å
Structure data

72552

9y66

EMDB-72552, PDB-9y66:
attLsym bound serine integrase complex in the dimeric state
Method: EM (single particle) / Resolution: 3.31 Å

72632

9y6v

EMDB-72632, PDB-9y6v:
attPsym bound large serine integrase and RDF complex in the dimeric state
Method: EM (single particle) / Resolution: 7.1 Å

Chemicals

ChemComp-ZN:
Unknown entry

Source
  • spbetavirus spbeta
KeywordsRECOMBINATION / Site-specific DNA Recombinase / Large serine integrase / DNA binding domains / Recombinase / Resolvase / Zinc ribbon recombinase

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