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- W1946362544 endingPage "871" @default.
- W1946362544 startingPage "860" @default.
- W1946362544 abstract "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." @default.
- W1946362544 created "2016-06-24" @default.
- W1946362544 creator A5037292050 @default.
- W1946362544 creator A5039868655 @default.
- W1946362544 date "2015-08-01" @default.
- W1946362544 modified "2023-10-15" @default.
- W1946362544 title "An Atypical AAA+ ATPase Assembly Controls Efficient Transposition through DNA Remodeling and Transposase Recruitment" @default.
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- W1946362544 doi "https://doi.org/10.1016/j.cell.2015.07.037" @default.
- W1946362544 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4537775" @default.
- W1946362544 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/26276634" @default.
- W1946362544 hasPublicationYear "2015" @default.
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