Variations of sequences and amino acid compositions of proteins that sustain their biological functions: An analysis of the cyclophilin family of proteins
Variations of sequences and amino acid compositions of proteins that sustain their biological functions: An analysis of the cyclophilin family of proteins
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DOI：
10.1006/abbi.1999.1434
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发表时间：
1999-11-15
影响因子：
3.9
通讯作者：
Galat, A
中科院分区：
文献类型：
--
作者：
Galat, A
普遍存在且系统发育多样的亲环蛋白家族的序列被划分为6类，即脊椎动物、无脊椎动物、其他后生动物、植物、真菌和原核生物。利用多序列比对程序Clustal-W对这些序列进行比对。使用一套新颖的多序列比对分析程序，计算了这六组亲环蛋白的氨基酸取代和氨基酸组成的变化。来自脊椎动物的亲环蛋白可以分为至少两个不同的结构类，它们之间的不同之处在于连接α -螺旋II和β -链III的环内插入了一个可变长度的氨基酸。类似的结构特征也存在于其他类群的亲环蛋白中，即来自无脊椎动物、其他后生动物、植物和真菌的亲环蛋白。来自真菌和原核生物的亲环蛋白序列比来自脊椎动物的亲环蛋白更多样化，它们的改变涉及到环内插入的氨基酸以外的结构。计算了每组亲环蛋白和所有序列的亲疏水性和氨基酸取代量的变化。这些变化具有明显的不对称性，这可能意味着在进化环境中与各种细胞成分相互作用的亲环蛋白的某些片段的物理性质需要修改。(C) 1999学术出版社。
The sequences of the ubiquitous and phylogenetically diversified cyclophilin family of proteins were divided into six groups, namely, vertebrates, invertebrates, other metazoa, plants, fungi, and prokaryotes. These groups of sequences were aligned with the multiple sequence alignment program Clustal-W. The variations of amino acid substitutions and amino acid compositions for these six groups of cyclophilins were calculated using a novel suite of multiple-sequence alignment analysis routines. The cyclophilins from vertebrates can be divided for at least two distinct structural classes that differ from each other by a variable-length amino acid insert within the loop that links alpha-helix II and beta-strand III. A similar structural feature is also present in the other groups of cyclophilins, namely, those from invertebrates, other metazoa, plants, and fungi. The sequences of cyclophilins from fungi and prokaryotes are more diversified than those from vertebrates, and their alterations involve structures other than the amino acid inserts within the loops. Variations of the hydrophobicity and bulkiness of amino acid substitutions of the aligned sequences were calculated for each group of cyclophilins and for the alignment of all the sequences. The variations have clear asymmetry that may signify the need for modification of the physical properties of certain fragments of cyclophilins that are involved in interactions with various cellular components in the evolving environment. (C) 1999 Academic Press.