Garcia-Robles Inmaculada, Akarsu Hatice, Müller Christoph W, Ruigrok Rob W H, Baudin Florence
EMBL Grenoble Outstation, BP 181, 38042 Grenoble Cedex 9, France.
Virology. 2005 Feb 5;332(1):329-36. doi: 10.1016/j.virol.2004.09.036.
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.
在流感病毒感染期间,病毒RNA的转录和复制在细胞核中进行。病毒核糖核蛋白(RNPs,包含vRNA、核蛋白和病毒聚合酶的病毒亚基)进入细胞核后,会立即与核基质紧密结合。在此,我们分析了RNPs、M1和NS2/NEP蛋白与纯化的核小体、重组组蛋白八聚体和纯化的单个组蛋白的结合情况。RNPs和M1都与染色质成分结合,但结合位点不同,RNPs结合到组蛋白尾部,M1结合到组蛋白八聚体的球状结构域。NS2/NEP根本不与核小体结合。本文讨论了这些发现对于新合成的RNPs从细胞核释放以及感染周期中其他过程的可能影响。