Interaction of influenza virus proteins with nucleosomes.
During influenza virus infection, transcription and replication of the viral RNA take place in the cell nucleus. Directly after entry in the nucleus the viral ribonucleoproteins (RNPs, the viral subunits containing vRNA, nucleoprotein and the viral polymerase) are tightly associated with the nuclear matrix. Here, we have analysed the binding of RNPs, M1 and NS2/NEP proteins to purified nucleosomes, reconstituted histone octamers and purified single histones. RNPs and M1 both bind to the chromatin components but at two different sites, RNP to the histone tails and M1 to the globular domain of the histone octamer. NS2/NEP did not bind to nucleosomes at all. The possible consequences of these findings for nuclear release of newly made RNPs and for other processes during the infection cycle are discussed.
Garcia-Robles
Inmaculada
I
EMBL Grenoble Outstation, BP 181, 38042 Grenoble Cedex 9, France.
Akarsu
Hatice
H
Müller
Christoph W
CW
Ruigrok
Rob W H
RW
Baudin
Florence
F
D000818:Animals; D006657:Histones / Q000032:analysis / Q000737:chemistry; D009698:Nucleoproteins / Q000378:metabolism; D009707:Nucleosomes / Q000378:metabolism*; D009975:Orthomyxoviridae / Q000378:metabolism*; D011485:Protein Binding; D012261:Ribonucleoproteins / Q000378:metabolism; D014764:Viral Proteins / Q000378:metabolism*; D014981:Xenopus
D006657:Histones; D009698:Nucleoproteins; D009707:Nucleosomes; D012261:Ribonucleoproteins; D014764:Viral Proteins