Unknown

Dataset Information

0

Structural basis of transposon end recognition explains central features of Tn7 transposition systems.


ABSTRACT: 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.

SUBMITTER: Kaczmarska Z 

PROVIDER: S-EPMC9308760 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC4105704 | biostudies-literature
| S-EPMC3416591 | biostudies-literature
| S-EPMC6188088 | biostudies-literature
| S-EPMC3114436 | biostudies-literature
| S-EPMC9080059 | biostudies-literature
| S-EPMC1855776 | biostudies-literature
| S-EPMC4423380 | biostudies-literature
| S-EPMC6904524 | biostudies-literature
| S-EPMC3156190 | biostudies-literature
| S-EPMC8571069 | biostudies-literature