Dingwall C, Dilworth S M, Black S J, Kearsey S E, Cox L S, Laskey R A
EMBO J. 1987 Jan;6(1):69-74. doi: 10.1002/j.1460-2075.1987.tb04720.x.
Nucleoplasmin is the most abundant protein in the Xenopus oocyte nucleus. It is involved in histone storage and chromatin assembly and it has been used extensively to study the transport of proteins into the cell nucleus. We have isolated lambda gt11 phage containing nucleoplasmin cDNA and have determined the sequence of the entire protein coding region of 200 amino acids for one of the two genes. The translation product of the sp6 transcript of this cDNA has the same electrophoretic mobility as nucleoplasmin and is able to form pentamers. The protein sequence shows remarkable clusters of charged residues including a long polyglutamic acid tract which presumably constitutes the histone binding site. The short C-terminal domain which specifies nuclear entry contains four regions which are homologous to putative nuclear localization signals including two regions of homology to the nuclear migration signal of SV40 large T antigen.
核质蛋白是非洲爪蟾卵母细胞核中含量最丰富的蛋白质。它参与组蛋白的储存和染色质组装，并且已被广泛用于研究蛋白质向细胞核的转运。我们分离出了含有核质蛋白cDNA的λgt11噬菌体，并确定了两个基因之一的200个氨基酸的整个蛋白质编码区的序列。该cDNA的sp6转录本的翻译产物具有与核质蛋白相同的电泳迁移率，并且能够形成五聚体。蛋白质序列显示出明显的带电残基簇，包括一个长的聚谷氨酸序列，推测它构成组蛋白结合位点。指定核进入的短C末端结构域包含四个与假定的核定位信号同源的区域，包括与SV40大T抗原的核迁移信号同源的两个区域。
