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TitleStructural basis of transposon end recognition explains central features of Tn7 transposition systems.
Journal, issue, pagesMol Cell, Vol. 82, Issue 14, Page 2618-22632.e7, Year 2022
Publish dateJul 21, 2022
AuthorsZuzanna Kaczmarska / Mariusz Czarnocki-Cieciura / Karolina M Górecka-Minakowska / Robert J Wingo / Justyna Jackiewicz / Weronika Zajko / Jarosław T Poznański / Michał Rawski / Timothy Grant / Joseph E Peters / Marcin Nowotny /
PubMed AbstractTn7 is a bacterial transposon with relatives containing element-encoded CRISPR-Cas systems mediating RNA-guided transposon insertion. Here, we present the 2.7 Å cryoelectron microscopy structure of ...Tn7 is a bacterial transposon with relatives containing element-encoded CRISPR-Cas systems mediating RNA-guided transposon insertion. Here, we present the 2.7 Å cryoelectron microscopy structure of prototypic Tn7 transposase TnsB interacting with the transposon end DNA. When TnsB interacts across repeating binding sites, it adopts a beads-on-a-string architecture, where the DNA-binding and catalytic domains are arranged in a tiled and intertwined fashion. The DNA-binding domains form few base-specific contacts leading to a binding preference that requires multiple weakly conserved sites at the appropriate spacing to achieve DNA sequence specificity. TnsB binding imparts differences in the global structure of the protein-bound DNA ends dictated by the spacing or overlap of binding sites explaining functional differences in the left and right ends of the element. We propose a model of the strand-transfer complex in which the terminal TnsB molecule is rearranged so that its catalytic domain is in a position conducive to transposition.
External linksMol Cell / PubMed:35654042 / PubMed Central
MethodsEM (single particle) / EM (helical sym.)
Resolution2.68 - 3.79 Å
Structure data

13439

7pik

EMDB-13439, PDB-7pik:
Cryo-EM structure of E. coli TnsB in complex with right end fragment of Tn7 transposon
Method: EM (single particle) / Resolution: 2.68 Å

EMDB-13440: Cryo-EM helical reconstruction of E. coli TnsB in complex with right end fragment of Tn7 transposon
Method: EM (helical sym.) / Resolution: 3.79 Å

Source
  • escherichia coli (E. coli)
KeywordsDNA BINDING PROTEIN / complex / nuclease / Tn7 / transposon

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