The DExD-box RNA helicase Dbp7 unwinds short double-stranded RNAs
DExD-box proteins are ATP-dependent enzymes that unwind double-stranded RNAs in a non-processive manner, often initiating strand separation from 5′- or 3′-single-stranded overhangs. Dbp7, a member of this family, is required for yeast ribosome biogenesis and has been specifically implicated in the r...
| Autores: | , , , , , , |
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| Formato: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 2026 |
| País: | España |
| Recursos: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/422720 |
| Acesso em linha: | http://hdl.handle.net/10261/422720 https://api.elsevier.com/content/abstract/scopus_id/105029947507 |
| Access Level: | acceso abierto |
| Palavra-chave: | DEAD-box protein Dbp7 RNA binding RNA helicase Ribosome biogenesis Saccharomyces cerevisiae |
| Resumo: | DExD-box proteins are ATP-dependent enzymes that unwind double-stranded RNAs in a non-processive manner, often initiating strand separation from 5′- or 3′-single-stranded overhangs. Dbp7, a member of this family, is required for yeast ribosome biogenesis and has been specifically implicated in the release of the small nucleolar RNA snR190 from early pre-60S particles. To gain mechanistic insight into its function, we have examined the in vitro helicase activity of recombinant Dbp7. We show that it efficiently unwinds short double-stranded RNA substrates in an ATP-dependent manner, irrespective of overhang polarity, thereby establishing it as a bona fide DExD-box RNA helicase. |
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