Fagan M B, Weissman I L
Stanford University, Department of Pathology, Stanford University Medical Center, Stanford, CA 94305, USA.
Immunogenetics. 1996;44(2):134-42. doi: 10.1007/BF02660062.
Two genes belonging to the heat shock protein 70 gene family have been cloned from the colonial protochordate Botryllus schlosseri. The two intronless genes (HSP70.1 and HSP70.2) exhibit 93.6% sequence identity within the predicted coding region, and 83.3% and 81.7% sequence identity in the 5' and 3' flanking regions, respectively. The predicted amino acid sequences are 95% identical and contain several signatures characteristic of cytoplasmic eukaryotic HSP70 genes (Gupta et al. 1994; Rensing and Maier 1994). Northern blotting and sequence analysis suggest that both genes are heat-inducible members of the HSP70 gene family. Given these characteristics, HSP70.1 and HSP70.2 appear to be good candidates for protochordate homologues of the major histocompatibility complex-linked HSP70 genes of human, mouse, and rat (Milner and Campbell 1990; Walter et al. 1994). Further experiments to determine whether there is functional evidence for such similarity are in progress.
已从群体原索动物柄海鞘中克隆出两个属于热休克蛋白70基因家族的基因。这两个无内含子基因(HSP70.1和HSP70.2)在预测的编码区域内表现出93.6%的序列同一性,在5'和3'侧翼区域的序列同一性分别为83.3%和81.7%。预测的氨基酸序列有95%相同,并包含几个细胞质真核热休克蛋白70基因的特征性序列(古普塔等人,1994年;伦辛和迈尔,1994年)。Northern印迹法和序列分析表明,这两个基因都是热休克蛋白70基因家族的热诱导成员。鉴于这些特征,HSP70.1和HSP70.2似乎是人类、小鼠和大鼠主要组织相容性复合体相关热休克蛋白70基因的原索动物同源物的良好候选者(米尔纳和坎贝尔,1990年;沃尔特等人,1994年)。确定这种相似性是否有功能证据的进一步实验正在进行中。