Cordes V, Waizenegger I, Krohne G
Institute of Cell and Tumor Biology, German Cancer Research Center, Heidelberg.
Eur J Cell Biol. 1991 Jun;55(1):31-47.
cDNA clones for nuclear pore complex glycoprotein p62 of two distantly related species, mouse and Xenopus laevis, were isolated. Antibodies raised against recombinant murine p62 react on protein blots with p62 of both species and decorate pore complexes. Analysis of the predicted protein sequence indicates that vertebrate p62 is organized into two structurally different regions. The entire carboxy-terminal half (86.7% identical amino acids) and the amino-terminal 56 amino acids (62.5% identity) have been highly conserved during evolution. The amino-terminal half contains several penta amino acid repeats and is able to form beta-sheets, whereas the carboxy-terminal half is predominantly organized in alpha-helical structures in part with heptad repeats typical for intermediate filament proteins. p62 of mouse and Xenopus is glycosylated by N-acetylglucosamine additions in the amino-terminal half. The region containing these potential glycosylation sites has been identified.
分离出了两个远缘物种（小鼠和非洲爪蟾）核孔复合体糖蛋白p62的cDNA克隆。针对重组鼠p62产生的抗体在蛋白质印迹上与这两个物种的p62发生反应，并对孔复合体进行标记。对预测的蛋白质序列分析表明，脊椎动物的p62由两个结构不同的区域组成。整个羧基末端的一半（86.7%的氨基酸相同）和氨基末端的56个氨基酸（62.5%的一致性）在进化过程中高度保守。氨基末端的一半包含几个五肽氨基酸重复序列，能够形成β折叠，而羧基末端的一半主要由α螺旋结构组成，部分具有中间丝蛋白典型的七肽重复序列。小鼠和非洲爪蟾的p62在氨基末端的一半通过添加N-乙酰葡糖胺进行糖基化。已鉴定出含有这些潜在糖基化位点的区域。
