id	author	title	date	pages	extension	mime	words	sentences	flesch	summary	cache	txt
cord-279432-aik5bo6o	Digard, Paul	Complex formation between influenza virus polymerase proteins expressed in Xenopus oocytes	1989-07-31		.txt	text/plain	4847	225	50	As seen in virus-infected cells, all three P proteins associated into an immunoprecipitable complex, suggesting that the system has considerable promise for the reconstruction of an active influenza RNA polymerase. In view of the fact that the P proteins must interact with RNA, it seemed possible that the high sedimentation values obtained for individually expressed PBl and PB2 (Fig. 4) and for complexes containing PBl and PB2 could have arisen from the polypeptides binding to RNA present in the lysate. Furthermore, RNase treatment of lysates containing individually expressed PB2 also failed to affect its sedimentation pattern (not shown), suggesting that the heterogeneous size distribution of the P protein complexes is not the result of association with RNA. Here, we have demonstrated the feasibility of producing all three influenza virus polymerase proteins for functional studies by the translation of in vitro transcribed mRNA analogs in Xenopus oocytes. The three influenza virus polymerase (P) proteins not associated with viral nucleocapsids in the infected cell are in the form of a complex	./cache/cord-279432-aik5bo6o.txt	./txt/cord-279432-aik5bo6o.txt