从氨基酸残基的静态可及性探讨组蛋白的分子进化

AN EXPLORATION OF HISTONE MOLECULAR EVOLUTION FROM THE STATIC ACCESSIBILITY OF AMINO ACID RESIDUES

本文以蛋白质氨基酸残基的静态可及性为指标，分别探讨了Ｈ２Ａ、Ｈ２Ｂ、Ｈ３、Ｈ４这４种组蛋白分子的进化关系，并获得了Ｈ２Ａ、Ｈ２Ｂ和Ｈ３各自相应的分子系统树。该研究从分子进化的角度表明，在构成核小体的这４种组蛋白分子中，组蛋白Ｈ４的保守性最大。作者推测，与其他几种组蛋白相比，在维持染色体的结构、功能以及在染色体的起源上。

This paper investigated and discussed the evolutionary relations of four histone molecules,H2A,H2B,H3 and H4 with the static accessibilities of protein amino acid residues as an index The phylogenetic trees of H2A,H2B and H3 have been obtained The results indicated that protein three-dimensional structure is more reliable as studing protein molecular evolution;in addition, H4 is the most conservative protein in the four histone molecules composing nucleosome The authors speculate upon that histone H4,as compared with other histones,perhaps has the most important significance both in keeping chromosomal structure and function and in the origin of chromosome