Molecular basis for transposase activation by a dedicated AAA+ ATPase.

ABSTRACT: Transposases drive chromosomal rearrangements and the dissemination of drug-resistance genes and toxins^1-3. Although some transposases act alone, many rely on dedicated AAA+ ATPase subunits that regulate site selectivity and catalytic function through poorly understood mechanisms. Using IS21 as a model transposase system, we show how an ATPase regulator uses nucleotide-controlled assembly and DNA deformation to enable structure-based site selectivity, transposase recruitment, and activation and integration. Solution and cryogenic electron microscopy studies show that the IstB ATPase self-assembles into an autoinhibited pentamer of dimers that tightly curves target DNA into a half-coil. Two of these decamers dimerize, which stabilizes the target nucleic acid into a kinked S-shape

SUBMITTER: de la Gandara A 

PROVIDER: S-EPMC11208146 | biostudies-literature | 2024 Jun

REPOSITORIES: biostudies-literature