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TitleTransposon end recognition and excision mechanisms of type I-F CRISPR-associated transposases.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateMay 7, 2026
AuthorsMateusz Walter / Giada Finocchio / Seraina Oberli / Iana C Hammerschmid / George D Lampe / Julia Karan / Thomas Swartjes / Samuel H Sternberg / Martin Jinek / Irma Querques /
PubMed AbstractCRISPR-associated transposons (CASTs) are Tn7-like elements that have co-opted RNA-guided CRISPR effectors for targeted DNA insertion. CASTs have been adapted as genome editing tools for ...CRISPR-associated transposons (CASTs) are Tn7-like elements that have co-opted RNA-guided CRISPR effectors for targeted DNA insertion. CASTs have been adapted as genome editing tools for programmable, site-specific integration. Among them, the type I-F system from e (CAST) shows uniquely robust activity in human cells, yet its mechanistic basis remains poorly understood. Here, we present structural and biochemical analysis of the CAST transposase TnsAB. Biochemical reconstitution of transposon DNA excision defines key characteristics of the transposition mechanism. Cryogenic electron microscopy (cryo-EM) structures of TnsAB paired-end complexes reveal molecular determinants of transpososome assembly, transposon end recognition and cleavage. We validate these findings using biochemical and assays of structure-based transposase mutants, and provide mechanistic insights into the enhanced activity of a laboratory-evolved TnsAB variant. Together, our studies highlight molecular features underlying the efficiency of natural and engineered type I-F transposases and establish a mechanistic framework for their continued rational optimization.
External linksbioRxiv / PubMed:42146515 / PubMed Central
MethodsEM (single particle)
Resolution2.51 - 2.86 Å
Structure data

55638

9t7l

EMDB-55638, PDB-9t7l:
Cryo-EM structure of the PseTnsAB paired-end complex (right end) in the presence of Mg
Method: EM (single particle) / Resolution: 2.8 Å

57833

30jv

EMDB-57833, PDB-30jv:
Cryo-EM structure of the PseTnsAB paired-end complex (right end) in the presence of Mn
Method: EM (single particle) / Resolution: 2.86 Å

57834

30jw

EMDB-57834, PDB-30jw:
Cryo-EM structure of the PseTnsAB paired-end complex (left end) in the presence of Mg
Method: EM (single particle) / Resolution: 2.51 Å

Chemicals

ChemComp-MN:
Unknown entry

ChemComp-MG:
Unknown entry

Source
  • pseudoalteromonas sp. s983 (bacteria)
  • Pseudoalteromonas (bacteria)
KeywordsDNA BINDING PROTEIN / Transposase / DNA-binding / CRISPR-associated transposon / nuclease

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