MOLECULAR EVOLUTION OF THE Ca2+‐BINDING PHOTOPROTEINS OF THE HYDROZOA

MOLECULAR EVOLUTION OF THE Ca2+‐BINDING PHOTOPROTEINS OF THE HYDROZOA
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水生动物 Ca2+ 结合光蛋白的分子进化

DOI:
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发表时间:
1995
影响因子:
3.3
通讯作者:
S. Inouye
S. Inouye
中科院分区:
生物学3区
文献类型:
--
作者:
F. I. Tsuji;Y. Ohmiya;T. Fagan;H. Toh;S. Inouye

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水生动物光蛋白Aequorin、mitrocomin、clytin和obelin的一级结构比对显示出很强的氨基酸序列一致性。发现这些蛋白质的钙结合部位高度保守。这些钙结合位点也与其他钙结合蛋白的钙结合位点同源。然而,Aequorin、mitrocomin、clytin和obelin与其他钙结合蛋白不同,它们含有相对较多的半胱氨酸、色氨酸、组氨酸、Pro和酪氨酸残基,表明这些残基可能是作为发光机制的一部分而进化的。系统发育树的构建表明,水牛凝集素、丝裂原蛋白、粘连蛋白和方尖石蛋白形成了一组紧密相关的蛋白质。
Abstract— Alignment of the primary structures of the hydrozoan photoproteins, aequorin, mitrocomin, clytin and obelin showed very strong amino acid sequence identities. The Ca2+‐binding sites of the proteins were found to be highly conserved. The Ca2+‐binding sites were also homologous to the Ca2+‐binding sites of other Ca2+‐binding proteins. However, aequorin, mitrocomin, clytin and obelin differed from other Ca2+‐binding proteins in that they contained a relatively large number of cysteine, tryptophan, histidine, proline and tyrosine residues, suggesting that these residues may have evolved as part of the light‐emitting mechanism. Construction of a phylogenetic tree showed that aequorin, mitrocomin, clytin and obelin form a closely related group of proteins.
DOI: 10.1021/bi00539a041
发表时间: 1982-05
期刊: Biochemistry
影响因子: 2.9
作者:
T. Sasagawa;L. Ericsson;K. Walsh;W. E. Schreiber;E. Fischer;K. Titani
通讯作者: T. Sasagawa;L. Ericsson;K. Walsh;W. E. Schreiber;E. Fischer;K. Titani
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DOI: 10.1016/0076-6879(90)83042-8
发表时间: 1990
影响因子: --
作者:
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通讯作者: Gouy,M
DOI: --
发表时间: 1988
期刊: The Journal of biological chemistry
影响因子: --
作者:
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通讯作者: Theibert,JL