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Статья
Structural basis for the regulatory function of a complex zinc-binding domain in a replicative arterivirus helicase resembling a nonsense-mediated mRNA decay helicase
2021
All positive-stranded RNA viruses with genomes > ∼7 kb encode helicases, which generally are poorly characterized. The core of the nidovirus superfamily 1 helicase (HEL1) is associated with a unique N-terminal zinc-binding domain (ZBD) that was previously implicated in helicase regulation, genome replication and subgenomic mRNA synthesis. The high-resolution structure of the arterivirus helicase (nsp10), alone and in complex with a polynucleotide substrate, now provides first insights into the structural basis for nidovirus helicase function. A previously uncharacterized domain 1B connects HEL1 domains 1A and 2A to a long linker of ZBD, which further consists of a novel RING-like module and treble-clef zinc finger, together coordinating three Zn atoms. On substrate binding, major conformational changes were evident outside the HEL1 domains, notably in domain 1B. Structural characterization, mutagenesis and biochemistry revealed that helicase activity depends on the extensive relay of interactions between the ZBD and HEL1 domains. The arterivirus helicase structurally resembles the cellular Upf1 helicase, suggesting that nidoviruses may also use their helicases for post-transcriptional quality control of their large RNA genomes. © The Author(s) 2013.
Цитирование
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Версии
- 1. Version of Record от 2021-04-27
Метаданные
Название журнала
- Nucleic Acids Research
Том
- 42
Выпуск
- 5
Страницы
- 3464-3477
Ключевые слова
- adenosine triphosphatase; RNA helicase; alpha helix; Arterivirus; article; beta sheet; binding affinity; crystal structure; DNA binding; DNA conformation; enzyme active site; enzyme activity; enzyme assay; hydrogen bond; mutagenesis; nonhuman; nonsense mediated mRNA decay; nucleotide sequence; phenotype; priority journal; protein secondary structure; RNA synthesis; virus replication; Adenosine Triphosphatases; Arteritis Virus, Equine; DNA; Models, Molecular; Nonsense Mediated mRNA Decay; Protein Structure, Tertiary; RNA Helicases; Sequence Deletion; Viral Proteins; Zinc
Издатель
- Oxford University Press
Тип документа
- journal article
Тип лицензии Creative Commons
- CC
Правовой статус документа
- Свободная лицензия
Источник
- scopus
