Gonzalez P, Rao P V, Zigler J S
Laboratory of Mechanisms of Ocular Diseases, National Eye Institute, National Institutes of Health, Bethesda, Maryland 20892.
Genomics. 1994 May 15;21(2):317-24. doi: 10.1006/geno.1994.1272.
zeta-Crystallin is a protein highly expressed in the lens of guinea pigs and camels, where it comprises about 10% of the total soluble protein. It has recently been characterized as a novel quinone oxidoreductase present in a variety of mammalian tissues. We report here the isolation and characterization of the human zeta-crystallin gene (CRYZ) and its processed pseudogene. The functional gene is composed of nine exons and spans about 20 kb. The 5'-flanking region of the gene is rich in G and C (58%) and lacks TATA and CAAT boxes. Previous analysis of the guinea pig gene revealed the presence of two different promoters, one responsible for the high lens-specific expression and the other for expression at the enzymatic level in numerous tissues. Comparative analysis with the guinea pig gene shows that a region of approximately 2.5 kb that includes the promoter responsible for the high expression in the lens in guinea pig is not present in the human gene.
ζ-晶体蛋白是一种在豚鼠和骆驼晶状体中高度表达的蛋白质，在那里它占总可溶性蛋白质的约10%。最近它被鉴定为存在于多种哺乳动物组织中的一种新型醌氧化还原酶。我们在此报告人类ζ-晶体蛋白基因（CRYZ）及其加工假基因的分离和鉴定。功能基因由九个外显子组成，跨度约20kb。该基因的5'侧翼区域富含G和C（58%），缺乏TATA盒和CAAT盒。先前对豚鼠基因的分析揭示了存在两个不同的启动子，一个负责晶状体特异性高表达，另一个负责在许多组织中酶水平的表达。与豚鼠基因的比较分析表明，人类基因中不存在约2.5kb的区域，该区域包含负责豚鼠晶状体高表达的启动子。
