Ren Guoping, Stephan Daniel, Xu Zhaohui, Zheng Ying, Tang Danming, Harrison Rosemary S, Kurz Mareike, Jarrott Russell, Shouldice Stephen R, Hiniker Annie, Martin Jennifer L, Heras Begoña, Bardwell James C A
Howard Hughes Medical Institute, Departments of Molecular, Cellular, and Developmental Biology and Biological Chemistry, University of Michigan, Ann Arbor, Michigan 48109, USA.
J Biol Chem. 2009 Apr 10;284(15):10150-9. doi: 10.1074/jbc.M809509200. Epub 2009 Jan 30.
The ubiquitous thioredoxin fold proteins catalyze oxidation, reduction, or disulfide exchange reactions depending on their redox properties. They also play vital roles in protein folding, redox control, and disease. Here, we have shown that a single residue strongly modifies both the redox properties of thioredoxin fold proteins and their ability to interact with substrates. This residue is adjacent in three-dimensional space to the characteristic CXXC active site motif of thioredoxin fold proteins but distant in sequence. This residue is just N-terminal to the conservative cis-proline. It is isoleucine 75 in the case of thioredoxin. Our findings support the conclusion that a very small percentage of the amino acid residues of thioredoxin-related proteins are capable of dictating the functions of these proteins.
普遍存在的硫氧还蛋白折叠蛋白根据其氧化还原特性催化氧化、还原或二硫键交换反应。它们在蛋白质折叠、氧化还原控制和疾病中也起着至关重要的作用。在这里，我们已经表明，一个单一的残基强烈地改变了硫氧还蛋白折叠蛋白的氧化还原特性及其与底物相互作用的能力。这个残基在三维空间中与硫氧还蛋白折叠蛋白的特征CXXC活性位点基序相邻，但在序列上距离较远。这个残基就在保守的顺式脯氨酸的N端。在硫氧还蛋白的情况下，它是异亮氨酸75。我们的研究结果支持这样的结论，即硫氧还蛋白相关蛋白中非常小比例的氨基酸残基能够决定这些蛋白的功能。
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