Characterization of a temperature-sensitive mutant in the RNA polymerase PB2 subunit gene of influenza A/WSN/33 virus
Identifieur interne : 002121 ( Main/Exploration ); précédent : 002120; suivant : 002122Characterization of a temperature-sensitive mutant in the RNA polymerase PB2 subunit gene of influenza A/WSN/33 virus
Auteurs : K. Yamanaka [Japon] ; N. Ogasawara [Japon] ; M. Ueda [Japon] ; H. Yoshikawa [Japon] ; A. Ishihama [Japon] ; K. Nagata [Japon]Source :
- Archives of Virology [ 0304-8608 ] ; 1990-03-01.
English descriptors
- Teeft :
- Amino, Amino acid, Amino acid change, Amino acid changes, Amino acid number, Amino acid sequence, Amino acid sequences, Amino acids, Arch virol, Binding proteins, Catalytic unit, Cdna, Chain elongation, Complete nucleotide sequence, Consensus sequence, Creatine kinase, Creatine phosphate, Essential role, Final volume, Fourth sequence, Human influenza virus, Influenza, Influenza virus, Influenza viruses, Mdck cells, Molecular genetics, Mrna protein, Mutant, Mutation sites, National institute, Negative polarity, Nucleotide, Nucleotide sequence, Nucleotide sequence analysis, Polymerase, Polymerase chain reaction, Polymerase complexes, Positive polarity, Preliminary characterization, Primer, Proc natl acad, Rnase inhibitor, Temperature sensitivity, Third sequence, Ueda, Various influenza, Viral, Virion, Virol, Wild type, Wild type strain.
Abstract
Summary: The temperature-sensitive mutant ts-1 of influenza virus A/WSN/33 carries mutations in the gene encoding RNA polymerase PB2 subunit. Effect of temperature on various steps of viral RNA synthesis was examined using disrupted virions of ts-1 mutant. The initiation of RNA synthesis with dinucleotide ApG primer was not affected by elevated temperature, whereas that with primer RNA containing 5′-terminal cap-1 structure was temperature-sensitive. The result supports the previous notion deduced from the UV-crosslinking experiments, that PB2 is involved in the cap-1 dependent initiation of RNA synthesis. In addition, the ts-1 mutant showed a defect in RNA chain elongation. Nucleotide sequence analysis of RNA segment 1 of ts-1 mutant revealed that the amino acid number 417 is essential for the recognition of cap-1 structures and/or the interaction with catalytic unit of the RNA polymerase.
Url:
DOI: 10.1007/BF01311012
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">Summary: The temperature-sensitive mutant ts-1 of influenza virus A/WSN/33 carries mutations in the gene encoding RNA polymerase PB2 subunit. Effect of temperature on various steps of viral RNA synthesis was examined using disrupted virions of ts-1 mutant. The initiation of RNA synthesis with dinucleotide ApG primer was not affected by elevated temperature, whereas that with primer RNA containing 5′-terminal cap-1 structure was temperature-sensitive. The result supports the previous notion deduced from the UV-crosslinking experiments, that PB2 is involved in the cap-1 dependent initiation of RNA synthesis. In addition, the ts-1 mutant showed a defect in RNA chain elongation. Nucleotide sequence analysis of RNA segment 1 of ts-1 mutant revealed that the amino acid number 417 is essential for the recognition of cap-1 structures and/or the interaction with catalytic unit of the RNA polymerase.</div>
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