Berrios M, Fisher P A
J Cell Biol. 1986 Sep;103(3):711-24. doi: 10.1083/jcb.103.3.711.
A high molecular weight polypeptide, identified as an ATPase subunit by direct ultraviolet photoaffinity labeling, has been shown to be a component of nuclear envelope-enriched fractions prepared from a variety of higher eukaryotes (Berrios, M., G. Blobel, and P. A. Fisher, 1983, J. Biol. Chem., 258:4548-4555). In rat liver as well as Drosophila melanogaster embryos, this polypeptide appears to be a form of myosin heavy chain. This conclusion is based on both immunochemical and immunocytochemical data, as well as on the results of CNBr and chymotryptic peptide map analyses. In Drosophila, the identification of this myosin heavy chain-like polypeptide as a nuclear envelope component has been corroborated in situ by indirect immunofluorescence analyses using permeabilized whole cells, mechanically extruded nuclei, and cryosections obtained from a number of larval tissues. Localization appears to be restricted to the nuclear periphery in a manner similar to that observed for the nuclear lamins and the pore complex glycoprotein. Antibodies directed against the Drosophila nuclear envelope ATPase have also been shown to decorate mammalian and higher plant cell nuclei in situ. Implications for intracellular nuclear mobility and for nucleocytoplasmic exchange of macromolecules in vivo are discussed.
一种通过直接紫外光亲和标记鉴定为ATP酶亚基的高分子量多肽，已被证明是从多种高等真核生物制备的富含核膜的组分中的一种成分（贝里奥斯，M.，G.布洛贝尔，和P.A.费舍尔，1983，《生物化学杂志》，258:4548 - 4555）。在大鼠肝脏以及黑腹果蝇胚胎中，这种多肽似乎是肌球蛋白重链的一种形式。这一结论基于免疫化学和免疫细胞化学数据，以及基于溴化氰和胰凝乳蛋白酶肽图谱分析的结果。在果蝇中，通过使用透化的全细胞、机械挤压的细胞核以及从多个幼虫组织获得的冷冻切片进行间接免疫荧光分析，已在原位证实这种类肌球蛋白重链多肽作为核膜成分的身份。定位似乎局限于核周边，其方式类似于观察到的核纤层蛋白和孔复合体糖蛋白的定位方式。针对果蝇核膜ATP酶的抗体也已被证明能在原位标记哺乳动物和高等植物细胞核。文中讨论了其对细胞内核移动性以及体内大分子核质交换的意义。
