期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 5, 页码 3464-3477出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkt1310
关键词
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资金
- National Basic Research Program of China [973 Program] [2011CB965304, 2009CB825501]
- National Natural Science Foundation of China [31370720, 31222032, 90919043, 31070664]
- Chinese Universities Scientific Fund [2013QJ027]
- Specialized Research Fund for the Doctoral Program of Higher Education [20100008 110009]
- Open Research Fund Program of the State Key Laboratory of Virology of China [2013IOV003]
- National Laboratory of Medical Molecular Biology (PUMC)
- European Union [264286]
- Netherlands Organization for Scientific Research [NWO] [TOP-GO 700.10.352]
- Leiden University Medical Center
- Moscow State University (MoBiLe)
- Leiden University
All positive-stranded RNA viruses with genomes >similar to 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.
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