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Structural basis for RNA-duplex unwinding by the DEAD-box helicase DbpA.
Wurm, Jan Philip.
Afiliação
  • Wurm JP; Institute of Biophysics and Physical Biochemistry, Regensburg Center for Biochemistry, University of Regensburg, 93053 Regensburg, Germany jan-philip.wurm@ur.de.
RNA ; 29(9): 1339-1354, 2023 09.
Article em En | MEDLINE | ID: mdl-37221012
DEAD-box RNA helicases are implicated in most aspects of RNA biology, where these enzymes unwind short RNA duplexes in an ATP-dependent manner. During the central step of the unwinding cycle, the two domains of the helicase core form a distinct closed conformation that destabilizes the RNA duplex, which ultimately leads to duplex melting. Despite the importance of this step for the unwinding process no high-resolution structures of this state are available. Here, I used nuclear magnetic resonance spectroscopy and X-ray crystallography to determine structures of the DEAD-box helicase DbpA in the closed conformation, complexed with substrate duplexes and single-stranded unwinding product. These structures reveal that DbpA initiates duplex unwinding by interacting with up to three base-paired nucleotides and a 5' single-stranded RNA duplex overhang. These high-resolution snapshots, together with biochemical assays, rationalize the destabilization of the RNA duplex and are integrated into a conclusive model of the unwinding process.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: RNA Helicases DEAD-box Idioma: En Ano de publicação: 2023 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: RNA Helicases DEAD-box Idioma: En Ano de publicação: 2023 Tipo de documento: Article