The Journal of Biochemistry
Online ISSN : 1756-2651
Print ISSN : 0021-924X
RNA Polymerase of Influenza Virus: Role of NP in RNA Chain Elongation
Ayae HondaKenji UédaKyosuke NagataAkira Ishihama
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1988 Volume 104 Issue 6 Pages 1021-1026

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Abstract

Ribonucleoprotein (RNP) cores of influenza virus A/PR/8/34 were dissociated into RNA
polymerase (PB1-PB2-PA complex)-associated genome RNA and nuclear protein (NP) fractions by CsC1 centrifugation. The RNA polymerase-RNA complexes were capable of catalyzing the endonucleolytic cleavage of capped RNA, the initiation of primer-dependent RNA synthesis, and the synthesis of small-sized RNA, but were unable to synthesize template-sized RNA. By adding the NP protein to the RNA polymerase-RNA complexes, RNP (RNA polymerase-RNA-NP) complexes were reconstituted; they synthesized template-sized transcripts as did native RNP cores. These observations are consistent with the model where viral RNA polymerase is composed of the three P proteins while NP is essential for the elongation of RNA chains. RNP was completely dissociated into RNA-free proteins (PB1, PB2, PA, and NP) and a protein-free genome RNA fraction by centrifugation in cesium trifluoroacetate (CsTFA) and glycerol. By mixing the protein and RNA fractions, primer-dependent RNA-synthesizing activity was regained. These complexes, however, produced only small-sized RNA, presumably due to incorrect assembly of NP on viral RNA.

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© The Japanese Biochemical Society
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