期刊
JOURNAL OF VIROLOGY
卷 84, 期 4, 页码 2169-2175出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.02011-09
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资金
- Comision Interministerial de Ciencia y Tecnologia (CICYT) [BIO2007-60978]
- Conserjeria de Educacion y Cultura de la Comunidad de Madrid [S-SAL-0185/06]
- European Communities [EU-245141]
- National Pork Board [08-197]
- Consejo Superior de Investigaciones Cientificas (CSIC)
- Comunidad Autonoma de Madrid
Purified nucleocapsid protein (N protein) from transmissible gastroenteritis virus (TGEV) enhanced hammerhead ribozyme self-cleavage and favored nucleic acid annealing, properties that define RNA chaperones, as previously reported. Several TGEV N-protein deletion mutants were expressed in Escherichia coli and purified, and their RNA binding ability and RNA chaperone activity were evaluated. The smallest N-protein domain analyzed with RNA chaperone activity, facilitating DNA and RNA annealing, contained the central unstructured region (amino acids 117 to 268). Interestingly, N protein and its deletion mutants with RNA chaperone activity enhanced template switching in a retrovirus-derived heterologous system, reinforcing the concept that TGEV N protein is an RNA chaperone that could be involved in template switching. This result is in agreement with the observation that in vivo, N protein is not necessary for TGEV replication, but it is required for efficient transcription.
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