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  • Title: Molecular assembly of the influenza virus RNA polymerase: determination of the subunit-subunit contact sites.
    Author: Toyoda T, Adyshev DM, Kobayashi M, Iwata A, Ishihama A.
    Journal: J Gen Virol; 1996 Sep; 77 ( Pt 9)():2149-57. PubMed ID: 8811014.
    Abstract:
    Influenza virus RNA polymerase with the subunit structure PB1-PB2-PA is involved in both transcription and replication of the RNA genome. By transfection of various combinations of cDNA encoding wild-type and serial deletion mutants of each P protein subunit and co-immunoprecipitation with subunit-specific antibodies, the subunit-subunit contact sites on all three of the P proteins were determined. Results indicate that binary complexes are formed between PB1-PB2 and PB1-PA but not between PB2-PA. Therefore, we concluded that PB1 is the core subunit for assembly of the virus RNA polymerase. The C-terminal 158 amino acids of PB1 bound to the N-terminal 249 amino acids of PB2, while the N-terminal 140 amino acids of PB1 bound to the C-terminal two-thirds of PA. PB2-PA binding was not detected when they were expressed in the absence of the PB1 subunit.
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