Chen M S, Roti J R, Laszlo A
Section of Cancer Biology, Radiation Oncology Center, Washington University School of Medicine, St. Louis, MO 63108, USA.
Gene. 1999 Oct 1;238(2):333-41. doi: 10.1016/s0378-1119(99)00333-9.
Here, we report the identification and characterization of a new hsp40 family member, heat shock cognate 40 (hsc40), which may be a specific functional partner for hsc70. The hsc40 gene consists of five exons and four introns. The previously characterized hsp40 gene contains only three exons and two introns. Despite this difference in the numbers of exons and introns, the structures of these two genes are actually quite similar. If the first two exons and introns of the hsc40 gene are excluded, the rest is essentially the same as the whole hsp40 gene. The intron/exon boundaries of the hsc40 and hsp40 genes are conserved with respect to amino acid coding, indicating that the hsp40 gene might have arisen from a duplicated hsc40 gene, which developed a new transcription-regulatory mechanism in the second intron. Hsc40 is evolutionally conserved. There is over 95% sequence identity between the putative mouse and human hsc40 proteins. However, there is only 60% sequence identity between the hsc40 and hsp40 proteins from either human or mouse cells. Northern blot analysis of various tissues and cells in culture revealed that this gene was expressed under normal conditions, and its expression was further increased after various stress treatments. The expression pattern of the hsc40 gene is very similar to that of the hsc70 gene under both normal and stress conditions, whereas the hsp40 gene exhibited an expression pattern more similar to that of hsp70 genes on the same Northern blots. These results, considered along with the high rate of sequence conservation between the same proteins from different species and high rate of variation between the two different proteins from the same species, strongly suggest that hsc40 and hsp40 may perform different functions and/or have different specificities in the cell.
在此,我们报告了一种新的热休克蛋白40(hsp40)家族成员——热休克同源蛋白40(hsc40)的鉴定与特性,它可能是hsc70的特定功能伙伴。hsc40基因由五个外显子和四个内含子组成。先前鉴定的hsp40基因仅包含三个外显子和两个内含子。尽管外显子和内含子数量存在差异,但这两个基因的结构实际上非常相似。如果排除hsc40基因的前两个外显子和内含子,其余部分与整个hsp40基因基本相同。hsc40和hsp40基因的内含子/外显子边界在氨基酸编码方面是保守的,这表明hsp40基因可能起源于复制的hsc40基因,该基因在第二个内含子中形成了一种新的转录调控机制。hsc40在进化上是保守的。推测的小鼠和人类hsc40蛋白之间的序列同一性超过95%。然而,来自人类或小鼠细胞的hsc40和hsp40蛋白之间的序列同一性仅为60%。对各种组织和培养细胞的Northern印迹分析表明,该基因在正常条件下表达,并且在各种应激处理后其表达进一步增加。在正常和应激条件下,hsc40基因的表达模式与hsc70基因非常相似,而在同一Northern印迹上,hsp40基因的表达模式与hsp70基因更相似。这些结果,结合来自不同物种的相同蛋白之间的高序列保守率以及来自同一物种的两种不同蛋白之间的高变异率,强烈表明hsc40和hsp40可能在细胞中执行不同的功能和/或具有不同的特异性。