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溶菌酶和α-乳白蛋白的进化

The evolution of lysozyme and alpha-lactalbumin.

作者信息

Nitta K, Sugai S

机构信息

Department of Polymer Science, Faculty of Science, Hokkaido University, Japan.

出版信息

Eur J Biochem. 1989 Jun 1;182(1):111-8. doi: 10.1111/j.1432-1033.1989.tb14806.x.

Abstract

From the analysis of phylogenetic trees constructed from the amino acid sequences and metal-binding properties of various lysozymes c and alpha-lactalbumins, it was found that before the divergence of the lineages of birds and mammals, calcium-binding lysozyme diverged from non-calcium-binding lysozyme. alpha-Lactalbumin evolved from the calcium-binding lysozyme along the mammalian lineage after the divergence of birds and mammals. Rapid evolution took place, not in the process of acquisition of the activity of alpha-lactalbumin, but after the loss of lysozyme activity, due to the change in the distribution of selective pressure on each amino acid site. A general process for the change in function of a protein during evolution is suggested to be as follows: after duplication of the gene, one of their protein products acquires a new function, besides that already present; the old function is eventually lost.

摘要

通过对由各种溶菌酶c和α-乳白蛋白的氨基酸序列及金属结合特性构建的系统发育树进行分析,发现鸟类和哺乳动物谱系分化之前,钙结合溶菌酶与非钙结合溶菌酶发生了分化。α-乳白蛋白是在鸟类和哺乳动物分化之后,沿着哺乳动物谱系从钙结合溶菌酶进化而来的。快速进化并非发生在获得α-乳白蛋白活性的过程中,而是在溶菌酶活性丧失之后,这是由于每个氨基酸位点上选择压力分布的变化所致。进化过程中蛋白质功能变化的一般过程如下:基因复制后,其蛋白质产物之一除了已有的功能外,还获得了新功能;旧功能最终丧失。

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