Puvion-Dutilleul F, Chelbi-Alix M K, Koken M, Quignon F, Puvion E, de Thé H
Laboratoire Organisation Fonctionnelle du Noyau de l'UPR 9044 CNRS, Villejuif, France.
Exp Cell Res. 1995 May;218(1):9-16. doi: 10.1006/excr.1995.1125.
We have studied at the ultrastructural level the localization of PML protein in response to adenovirus infection in HeLa cells. In nuclei of noninfected cells or at the early stage of infection, PML accumulated at the border of nuclear bodies as previously described [Koken et al. (1994) EMBO J. 13, 1073-1083]. Interestingly, we demonstrate herein that PML is also a component of the interchromatin granule-associated zones, recently described structures containing U1 snRNP [Visa et al. (1993) Eur. J. Cell Biol. 60, 308-321], suggesting that PML protein might be involved in some steps of splicing events. However, as the infection progressed these two cellular PML-containing structures disappeared but significant amounts of PML accumulated within two virus-induced structures, essentially the clear amorphous inclusions, but also the protein crystals. Relocalization of this protein to virus-induced structures may reflect an inactivation of PML functions.
我们在超微结构水平上研究了人乳头瘤病毒（HeLa）细胞中腺病毒感染后早幼粒细胞白血病（PML）蛋白的定位。在未感染细胞的细胞核或感染早期，PML如先前所述[科肯等人（1994年）《欧洲分子生物学组织杂志》13卷，第1073 - 1083页]在核体边缘积累。有趣的是，我们在此证明PML也是染色质间颗粒相关区域的一个组成部分，该区域是最近描述的含有U1小核核糖核蛋白的结构[维萨等人（1993年）《欧洲细胞生物学杂志》60卷，第308 - 321页]，这表明PML蛋白可能参与了剪接事件的某些步骤。然而，随着感染的进展，这两种含有细胞PML的结构消失了，但大量的PML在两种病毒诱导的结构中积累，主要是透明无定形内含物，也有蛋白晶体。这种蛋白质重新定位于病毒诱导的结构可能反映了PML功能的失活。
