Involvement of the N-terminal portion of influenza virus RNA polymerase subunit PB1 in nucleotide recognition

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Abstract

The influenza virus PB1 protein functions as a catalytic subunit of the viral RNA-dependent RNA polymerase and contains the highly conserved motifs of RNA-dependent RNA polymerases together with putative nucleotide-binding sites. PB1 also binds to viral genomic RNAs and its replicative intermediates through the promoter regions. The detail function and interplay between functional domains are not clarified although a part of structures and functions of PB1 have been clarified. In this study, we analyzed the function of PB1 subunit in the sense of nucleotide recognition using ribavirin, which is a nucleoside analog and inhibits viral RNA synthesis of many RNA viruses including influenza virus. We screened ribavirin-resistant PB1 mutants from randomly mutated PB1 cDNA library using a mini-replicon assay, and we identified a single mutation at the amino acid position 27 of PB1 as an important residue for the nucleotide recognition.

Journal

  • Biochemical and biophysical research communications

    Biochemical and biophysical research communications 443(3), 975-979, 2014-01

    Elsevier Inc.

Keywords

Codes

  • NII Article ID (NAID)
    120005399277
  • NII NACSIS-CAT ID (NCID)
    AA00564395
  • Text Lang
    ENG
  • Article Type
    journal article
  • ISSN
    0006-291X
  • Data Source
    IR 
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