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TitleStructural insight into Tn3 family transposition mechanism.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 6155, Year 2022
Publish dateOct 18, 2022
AuthorsAlexander V Shkumatov / Nicolas Aryanpour / Cédric A Oger / Gérôme Goossens / Bernard F Hallet / Rouslan G Efremov /
PubMed AbstractTransposons are diverse mobile genetic elements that play the critical role as genome architects in all domains of life. Tn3 is a widespread family and among the first identified bacterial ...Transposons are diverse mobile genetic elements that play the critical role as genome architects in all domains of life. Tn3 is a widespread family and among the first identified bacterial transposons famed for their contribution to the dissemination of antibiotic resistance. Transposition within this family is mediated by a large TnpA transposase, which facilitates both transposition and target immunity. Howtever, a structural framework required for understanding the mechanism of TnpA transposition is lacking. Here, we describe the cryo-EM structures of TnpA from Tn4430 in the apo form and paired with transposon ends before and after DNA cleavage and strand transfer. We show that TnpA has an unusual architecture and exhibits a family specific regulatory mechanism involving metamorphic refolding of the RNase H-like catalytic domain. The TnpA structure, constrained by a double dimerization interface, creates a peculiar topology that suggests a specific role for the target DNA in transpososome assembly and activation.
External linksNat Commun / PubMed:36257990 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.6 Å
Structure data

13906

7qd4

EMDB-13906, PDB-7qd4:
Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with 100 bp long transposon end DNA
Method: EM (single particle) / Resolution: 2.9 Å

13908

7qd5

EMDB-13908, PDB-7qd5:
Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with 48 bp long transposon end DNA
Method: EM (single particle) / Resolution: 3.1 Å

13909

7qd6

EMDB-13909, PDB-7qd6:
Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in complex with strand-transfer like DNA product
Method: EM (single particle) / Resolution: 3.0 Å

13910

7qd8

EMDB-13910, PDB-7qd8:
Cryo-EM structure of Tn4430 TnpA transposase from Tn3 family in apo state
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • bacillus thuringiensis (bacteria)
KeywordsRECOMBINATION / DNA transposition / Tn3 family / antibiotic resistance / protein metamorphosis

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