RT Journal Article SR Electronic(1) A1 Toyoda, Tetsuya A1 Adyshev, Djanybek M. A1 Kobayashi, Makoto A1 Iwata, Akira A1 Ishihama, AkiraYR 1996 T1 Molecular Assembly of the Influenza Virus RNA Polymerase: Determination of the Subunit-Subunit Contact Sites JF Journal of General Virology, VO 77 IS 9 SP 2149 OP 2157 DO https://doi.org/10.1099/0022-1317-77-9-2149 PB Microbiology Society, SN 1465-2099, AB 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., UL https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-77-9-2149