Laliberté J F, Dagenais A, Filion M, Bibor-Hardy V, Simard R, Royal A
J Cell Biol. 1984 Mar;98(3):980-5. doi: 10.1083/jcb.98.3.980.
The lamins are the major components of the nuclear matrix and are known as lamins A, B, and C with Mr 72,000, 68,000, and 62,000 when analysed by SDS PAGE. These three polypeptides are very similar, as determined by polypeptide mapping and immunological reactivity. Lamins A and C are so homologous that a precursor-product relationship has been proposed. Using an antiserum against nuclear matrix proteins that specifically immunoprecipitates the three lamins, we examined their synthesis in the rabbit reticulocytes lysate. Four bands of Mr 62,000, 68,000, 70,000, and 74,000 were specifically immunoprecipitated when polysomes or polyadenylated RNA were translated in vitro. By two-dimensional gel electrophoresis, the 68,000- and the 62,000-mol-wt proteins were identified as lamins B and C, respectively, and the 74,000-mol-wt polypeptide had properties of a precursor of lamin A. The mRNAs of lamin C and of the putative precursor of lamin A were completely separated by gel electrophoresis under denaturing conditions, and their respective sizes were determined. These results suggest that lamin A is not a precursor of lamin C.
核纤层蛋白是核基质的主要成分,通过SDS - PAGE分析时,它们被称为核纤层蛋白A、B和C,分子量分别为72,000、68,000和62,000。通过多肽图谱分析和免疫反应性测定,这三种多肽非常相似。核纤层蛋白A和C的同源性很高,因此有人提出它们存在前体 - 产物关系。我们使用一种针对核基质蛋白的抗血清,该抗血清能特异性免疫沉淀这三种核纤层蛋白,在兔网织红细胞裂解物中检测了它们的合成情况。当在体外翻译多核糖体或聚腺苷酸化RNA时,分子量为62,000、68,000、70,000和74,000的四条带被特异性免疫沉淀。通过二维凝胶电泳,分子量为68,000和62,000的蛋白质分别被鉴定为核纤层蛋白B和C,分子量为74,000的多肽具有核纤层蛋白A前体的特性。在变性条件下通过凝胶电泳将核纤层蛋白C和推测的核纤层蛋白A前体的mRNA完全分离,并确定了它们各自的大小。这些结果表明核纤层蛋白A不是核纤层蛋白C的前体。