Dingwall C, Laskey R A
Medical Research Council, Laboratory of Molecular Biology, Cambridge, UK.
Semin Cell Biol. 1990 Feb;1(1):11-7.
Nucleoplasmin was the first protein to be described as a molecular chaperone. Studies of nucleoplasmin have resulted in advances in two areas of cell biology. Firstly, the pathway of nucleosome assembly in Xenopus oocytes and eggs has been elucidated and is the only assembly pathway known in detail. Nucleosome assembly represents the major chaperoning function of nucleoplasmin. Secondly, nucleoplasmin has been used to elucidate the transport of proteins into the nucleus, revealing a selective entry mechanism for nuclear proteins, passage through the nuclear pore complex, and a two-step mechanism of transport. The properties and functions of nucleoplasmin are reviewed, together with other proteins which are related either structurally or functionally to nucleoplasmin.
核质蛋白是首个被描述为分子伴侣的蛋白质。对核质蛋白的研究在细胞生物学的两个领域取得了进展。首先,非洲爪蟾卵母细胞和卵中核小体组装途径已被阐明,这是唯一已知的详细组装途径。核小体组装代表了核质蛋白的主要伴侣功能。其次,核质蛋白已被用于阐明蛋白质向细胞核的转运,揭示了核蛋白的选择性进入机制、通过核孔复合体的过程以及两步转运机制。本文综述了核质蛋白的特性和功能,以及在结构或功能上与核质蛋白相关的其他蛋白质。