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- W2321092373 abstract "How helicase families with a conserved catalytic ‘helicase core’ evolved to function on varied RNA and DNA substrates by diverse mechanisms remains unclear. Here, we used the helicase core of Mss116, a DEAD-box protein that utilizes ATP to locally unwind dsRNA, to investigate helicase specificity and mechanism. Previously, we found that the two RecA-like domains of the helicase core of Mss116 are in an extended ‘open state’ in the absence of substrates and recognize ATP and duplex RNA in a modular manner. Upon formation of a compact ‘closed state’ containing an ATPase active site, conserved motifs in the first domain promote the nonprocessive unwinding of short duplex substrates bound to the second domain by excluding one RNA strand and bending the other. In the present work, we define the molecular basis for the specificity of DEAD-box proteins. However, we also find that Mss116 has ambiguous substrate unwinding properties and interacts with a variety of NTPs and nucleic acids. The efficiency of unwinding correlates with the stability of the closed-state helicase core, a complex with nucleotide and nucleic acid that forms as duplexes are unwound. Crystal structures reveal that core stability is modulated by family-specific interactions that favor certain substrates. This suggests how present-day helicases diversified from an ancestral core with broad specificity by retaining core closure as a common catalytic mechanism while optimizing substrate-binding interactions for different cellular functions." @default.
- W2321092373 created "2016-06-24" @default.
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- W2321092373 date "2015-01-01" @default.
- W2321092373 modified "2023-09-25" @default.
- W2321092373 title "Insights into Helicase Evolution from the Specificity and Mechanism of a Dead-Box Protein" @default.
- W2321092373 doi "https://doi.org/10.1016/j.bpj.2014.11.1824" @default.
- W2321092373 hasPublicationYear "2015" @default.
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