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金属硫蛋白的多样性和分布在生命之树中:一种多功能蛋白质。

Metallothionein diversity and distribution in the tree of life: a multifunctional protein.

机构信息

Microbial Ecology, CNRS UMR 5557, UMR INRA 1418, Université Lyon1, Université de Lyon, F-69622 Villeurbanne, France.

出版信息

Metallomics. 2018 Nov 14;10(11):1549-1559. doi: 10.1039/c8mt00165k.

DOI:10.1039/c8mt00165k
PMID:30229264
Abstract

MTs are small cysteine-rich proteins that chelate metal ions such as Cu+ and Zn2+, and are widely distributed in several life domains, in particular the eukaryotic one. They are present in the following phyla: Opisthokonta (mainly Fungi and Metazoa), Chloroplastida, Alveolata (ciliates) and Excavata (Trichomonas) for Eukaryota and Cyanobacteria, Actinobacteria, Proteobacteria and Firmicutes for Bacteria. However, their absence in some phyla underlines that MTs are far from being fully known. The MT amino acid sequences show a great diversity of sizes and structures both in terms of cysteine motifs and organization of these motifs. This review also highlights the different oxidized, apoprotein and metalated forms of MTs, the diversity of interactions they can establish with different molecules and their central and multifunctional cellular role. We present MTs as a protein system that could be a hub in molecular interaction networks. Studying MTs as a hub in cellular interaction networks should provide new insights for a better understanding of MT functioning and cellular processes.

摘要

金属硫蛋白是富含半胱氨酸的小分子蛋白,能够螯合 Cu+ 和 Zn2+ 等金属离子,广泛存在于多个生命领域,尤其是真核生物中。它们存在于以下门中:后生动物(主要是真菌和原生动物)、叶绿体、纤毛(纤毛虫)和多孔(滴虫)等真核生物,以及蓝藻、放线菌、变形菌和厚壁菌等细菌。然而,某些门中缺乏 MT 表明,MT 的认识还远远不够全面。MT 的氨基酸序列在半胱氨酸基序及其组织方式方面表现出大小和结构的多样性。本文还重点介绍了 MT 的不同氧化、脱辅基蛋白和金属化形式、它们与不同分子建立的多样性相互作用,以及其在细胞中的中心和多功能作用。我们将 MT 视为一个蛋白质系统,它可能是分子相互作用网络的枢纽。将 MT 作为细胞相互作用网络的枢纽进行研究,应该能够为更好地理解 MT 的功能和细胞过程提供新的见解。

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