MOLECULAR-CLONING OF NUCLEOBINDIN, A NOVEL DNA-BINDING PROTEIN THAT CONTAINS BOTH A SIGNAL PEPTIDE AND A LEUCINE ZIPPER STRUCTURE
MOLECULAR-CLONING OF NUCLEOBINDIN, A NOVEL DNA-BINDING PROTEIN THAT CONTAINS BOTH A SIGNAL PEPTIDE AND A LEUCINE ZIPPER STRUCTURE
复制标题
DOI：
10.1016/s0006-291x(05)81503-7
复制
发表时间：
1992-08-31
影响因子：
3.1
通讯作者：
KANAI, Y
中科院分区：
文献类型：
--
作者：
MIURA, K;TITANI, K;KANAI, Y
我们以前曾报道，KML 1 -7细胞克隆从狼疮倾向的MRL/1小鼠产生的可溶性因子，优先扩大抗DNA抗体生产跨越H-2屏障。我们纯化了这个因子，一个55 kD的蛋白质，我们称之为核结合蛋白（Nuc），并获得了它的cDNA克隆。尽管Nuc基因编码信号肽，事实上，Nuc被鉴定为分泌蛋白，但Nuc具有DNA结合特性。从cDNA序列预测的推定多肽的特征信号肽，亮氨酸拉链结构和碱性氨基酸丰富的区域。通过缺失亮氨酸拉链结构或富含碱性氨基酸的区域，破坏了Nuc的DNA结合特性。Nuc的氨基酸序列在小鼠和人之间高度保守。我们讨论了Nuc在自身免疫中的可能作用。
We have previously reported that KML1-7 cells cloned from a lupus-prone MRL/1 mouse produced a soluble factor that preferentially expanded anti-DNA antibody production across the H-2 barrier. We purified this factor, a 55 kD protein that we termed nucleobindin (Nuc), and obtained its cDNA clone. Although the gene for Nuc encodes a signal peptide and, in fact, Nuc was identified as a secreted protein, Nuc had a DNA binding property. The putative polypeptide predicted from the cDNA sequence featured a signal peptide, a leucine zipper structure and a basic amino acid-rich region. The DNA-binding property of Nuc was destroyed by deletion of either the leucine zipper structure or the basic amino acid-rich region. The amino acid sequences of Nuc are highly conserved between mouse and human. We discuss the possible role of Nuc in autoimmunity.