Bozidis Petros, Lazaridis Ioannis, Pagoulatos Gerassimos N, Angelidis Charalampos E
Laboratory of General Biology, Medical School, University of Ioannina, Greece.
Eur J Biochem. 2002 Mar;269(5):1553-60. doi: 10.1046/j.1432-1033.2002.02807.x.
Dj2 is a member of the DnaJ family of proteins, which regulate the chaperoning function of the hsp70s. We isolated a monkey cDNA dj2 clone corresponding to the large mRNA species encoded by the gene. This mRNA differs from the small mRNA produced by the same gene in that it contains a long 3' untranslated region. Both messages were found to be equally stable and to produce the same protein, which is susceptible to farnesylation. Studies in mouse tissues and various cell lines revealed that these messages and their products are differentially expressed. Surprisingly, we found that only the nonfarnesylated form of dj2 is capable of translocating to the cell nucleus, especially after heat shock. Finally, based on protein interaction studies, our results indicate that dj2 is a specific partner for hsc70 and not for hsp70.
Dj2是DnaJ蛋白家族的成员，该家族调节热休克蛋白70（hsp70s）的伴侣功能。我们分离出了一个与该基因编码的大mRNA种类相对应的猴cDNA dj2克隆。这种mRNA与同一基因产生的小mRNA的不同之处在于它含有一个长的3'非翻译区。发现这两种信使RNA同样稳定，且产生相同的蛋白质，该蛋白质易于法尼基化。对小鼠组织和各种细胞系的研究表明，这些信使RNA及其产物的表达存在差异。令人惊讶的是，我们发现只有非法尼基化形式的dj2能够转运到细胞核，尤其是在热休克后。最后，基于蛋白质相互作用研究，我们的结果表明dj2是hsc70的特异性伴侣，而非hsp70的。
