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TitleMolecular basis for transposase activation by a dedicated AAA+ ATPase.
Journal, issue, pagesNature, Vol. 630, Issue 8018, Page 1003-1011, Year 2024
Publish dateJun 26, 2024
AuthorsÁlvaro de la Gándara / Mercedes Spínola-Amilibia / Lidia Araújo-Bazán / Rafael Núñez-Ramírez / James M Berger / Ernesto Arias-Palomo /
PubMed AbstractTransposases drive chromosomal rearrangements and the dissemination of drug-resistance genes and toxins. Although some transposases act alone, many rely on dedicated AAA+ ATPase subunits that ...Transposases drive chromosomal rearrangements and the dissemination of drug-resistance genes and toxins. 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-shaped configuration that engages the IstA transposase at the interface between the two IstB oligomers to form an approximately 1 MDa transpososome complex. Specific interactions stimulate regulator ATPase activity and trigger a large conformational change on the transposase that positions the catalytic site to perform DNA strand transfer. These studies help explain how AAA+ ATPase regulators-which are used by classical transposition systems such as Tn7, Mu and CRISPR-associated elements-can remodel their substrate DNA and cognate transposases to promote function.
External linksNature / PubMed:38926614 / PubMed Central
MethodsEM (single particle)
Resolution3.18 - 3.62 Å
Structure data

18136
EMDB entry, No image

EMDB-18136, PDB-8q3w:
ATP-bound IstB in complex to duplex DNA
Method: EM (single particle) / Resolution: 3.18 Å

18144
EMDB entry, No image

EMDB-18144, PDB-8q4d:
IstA-IstB(E167Q) Strand Transfer Complex
Method: EM (single particle) / Resolution: 3.62 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

Source
  • geobacillus stearothermophilus (bacteria)
KeywordsDNA BINDING PROTEIN / DNA Transposition / transposon / transpososome / AAA+ ATPases / target DNA / IS21 / IstB / Insertion sequence / cryo-electron microscopy. / DNA integration / holo-transpososome / IstA / DDE transposase / DDE domain / AAA+ ATPase / DNA strand transfer complex / STC

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