Genealogy of the α-crystallin -: small heat-shock protein superfamily
Genealogy of the α-crystallin -: small heat-shock protein superfamily
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DOI：
10.1016/s0141-8130(98)00013-0
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发表时间：
1998-05-01
影响因子：
8.2
通讯作者：
Leunissen, JAM
中科院分区：
文献类型：
--
作者：
de Jong, WW;Caspers, GJ;Leunissen, JAM
40个非常不同的代表性的α-晶状体蛋白-小热休克蛋白（α-Hsp）超家族的序列进行了比较。其特征性的80-100个残基的C-末端“α-晶状体蛋白结构域”包含从原核生物到真核生物高度保守的短的共有序列。此外，还有一些位置可以清楚地区分动物和非动物的α-Hsps。预测α-晶状体蛋白结构域由两个疏水β-折叠基序组成，由长度可变的亲水区域分隔。保守的α-晶状体蛋白结构域与可变的N-末端结构域和C-末端延伸的组合可能调节各种α-Hsps作为应激保护和结构寡聚蛋白的性质。系统发育重建表明，多个α-热休克蛋白已经存在于原核生物和真核生物的最后共同祖先。这表明在真核生物进化过程中，动物和非动物α-Hsps起源于不同的祖先基因拷贝。重复的基因复制导致大多数生物体中存在多种α-Hsps。(C)1998 Elsevier Science B. V.保留所有权利。
Sequences of 40 very diverse representatives of the alpha-crystallin-small heat-shock protein (alpha-Hsp) superfamily are compared. Their characteristic C-terminal 'alpha-crystallin domain' of 80-100 residues contains short consensus sequences that are highly conserved from prokaryotes to eukaryotes. There are, in addition, some positions that clearly distinguish animal from non-animal alpha-Hsps. The alpha-crystallin domain is predicted to consist of two hydrophobic beta-sheet motifs, separated by a hydrophilic region which is variable in length. Combination of a conserved alpha-crystallin domain with a variable N-terminal domain and C-terminal extension probably modulates the properties of the various alpha-Hsps as stress-protective and structural oligomeric proteins. Phylogeny reconstruction indicates that multiple alpha-Hsps were already present in the last common ancestor of pro- and eukaryotes. It is suggested that during eukaryote evolution, animal and non-animal alpha-Hsps originated from different ancestral gene copies. Repeated gene duplications gave rise to the multiple alpha-Hsps present in most organisms. (C) 1998 Elsevier Science B.V. All rights reserved.