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TitleAn Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment.
Journal, issue, pagesCell, Vol. 162, Issue 4, Page 860-871, Year 2015
Publish dateAug 13, 2015
AuthorsErnesto Arias-Palomo / James M Berger /
PubMed AbstractTransposons are ubiquitous genetic elements that drive genome rearrangements, evolution, and the spread of infectious disease and drug-resistance. Many transposons, such as Mu, Tn7, and IS21, require ...Transposons are ubiquitous genetic elements that drive genome rearrangements, evolution, and the spread of infectious disease and drug-resistance. Many transposons, such as Mu, Tn7, and IS21, require regulatory AAA+ ATPases for function. We use X-ray crystallography and cryo-electron microscopy to show that the ATPase subunit of IS21, IstB, assembles into a clamshell-shaped decamer that sandwiches DNA between two helical pentamers of ATP-associated AAA+ domains, sharply bending the duplex into a 180° U-turn. Biochemical studies corroborate key features of the structure and further show that the IS21 transposase, IstA, recognizes the IstB•DNA complex and promotes its disassembly by stimulating ATP hydrolysis. Collectively, these studies reveal a distinct manner of higher-order assembly and client engagement by a AAA+ ATPase and suggest a mechanistic model where IstB binding and subsequent DNA bending primes a selected insertion site for efficient transposition.
External linksCell / PubMed:26276634 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution2.1 - 16.0 Å
Structure data

EMDB-3031:
Cryo-EM structure of ATP-bound IstB in complex to duplex DNA
Method: EM (single particle) / Resolution: 8.5 Å

EMDB-3032:
Cryo-EM structure of ATP-bound IstB
Method: EM (single particle) / Resolution: 16.0 Å

PDB-5bq5:
Crystal structure of the IstB AAA+ domain bound to ADP-BeF3
Method: X-RAY DIFFRACTION / Resolution: 2.1 Å

Chemicals

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

ChemComp-MG:
Unknown entry

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

ChemComp-HOH:
WATER

Source
  • geobacillus stearothermophilus (bacteria)
  • synthetic construct (others)
KeywordsATP-binding protein / AAA+ / ATPase / transposition / DNA binding

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