在凝固和纤维溶解蛋白酶中保存的Ser残留的Codon切换
Bosko M Stojanovski1, Enrico Di Cera1
1Edward A. Doisy Department of Biochemistry and Molecular Biology, Saint Louis University School of Medicine, St Louis, Missouri, USA.
蛋白酶中使用的血清 (Ser) 密码体表明,基本残留物很少切换密码体,除了快速演变的鱼类基因. 非必需的Ser残留物经常会切换代码,特别是在环形域中.
科学领域:
- 生物化学 生物化学
- 进化生物学 进化生物学
- 基因组学就是基因组学.
背景情况:
- 血清素 (Ser) 是独一无二的,因为它是由两个编码子集 (TCN和AGY) 编码的,它们不会通过单核酸替代相互转换.
- 血清蛋白酶中的基本活性位点残留物 (S195,S214) 使用这些子,但由于突变后的活性损失,进化子相互转换机制仍然不清楚.
研究的目的:
- 研究脊椎动物凝血和纤维溶解蛋白酶中的必需和非必需Ser残留物中代码转换的频率.
- 了解关键蛋白酶家族中Ser编码子使用的进化动态.
主要方法:
- 分析TCN和AGY码头使用模式.
- 对来自不同脊椎动物血统的550多个蛋白质序列的检查.
主要成果:
- 绝对的进化压力维持了S195的子,没有观察到相互转换.
- 强大的压力也保留了S214编码子,尽管在快速演变的基因中,在特定的光鱼蛋白酶 (因子VII-不活跃,蛋白C) 中发现了AGYTCN相互转换.
- 阴切换在凝血和纤维溶解蛋白酶的 kringle 域内的非必需 Ser 残留中普遍存在,在大约一半的分析域中发生.
结论:
- 在凝血/纤维溶解蛋白酶中,对于必需的Ser残留物进行干间转换是罕见的,主要发生在快速演变的基因中,有时在基因组重复后发生.
- 对于非必需的Ser残留物,例如Kringle域中的Codons的相互转换是一种常见的进化事件.
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