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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states
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Mechanisms of protein oligomerization, the critical role of insertions and deletions in maintaining different oligomeric states

机译：蛋白质寡聚化的机制，插入和缺失在维持不同寡聚态中的关键作用

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摘要

The main principles of protein-protein recognition are elucidated by the studies of homooligomers which in turn mediate and regulate gene expression, activity of enzymes, ion channels, receptors, and cell-cell adhesion processes. Here we explore oligomeric states of homologous proteins in various organisms to better understand the functional roles and evolutionary mechanisms of homooligo-merization. We observe a great diversity in mechanisms controlling oligomerization and focus in our study on insertions and deletions in homologous proteins and how they enable or disable complex formation. We show that insertions and deletions which differentiate monomers and dimers have a significant tendency to be located on the interaction interfaces and about a quarter of all proteins studied and forty percent of enzymes have regions which mediate or disrupt the formation of oligomers. We suggest that relatively small insertions or deletions may have a profound effect on complex stability and/or specificity. Indeed removal of complex enabling regions from protein structures in many cases resulted in the complete or partial loss of stability. Moreover, we find that insertions and deletions modulating oligomerization have a lower aggregation propensity and contain a larger fraction of polar, charged residues, glycine and proline compared to conventional interfaces and protein surface. Most likely, these regions may mediate specific interactions, prevent nonspecific dysfunctional aggregation and preclude undesired interactions between close paralogs therefore separating their functional pathways. Last, we show how the presence or absence of insertions and deletions on interfaces might be of practical value in annotating protein oligomeric states.
机译：同源寡聚体的研究阐明了蛋白质-蛋白质识别的主要原理，而同源寡聚体又介导并调节基因表达，酶的活性，离子通道，受体和细胞间粘附过程。在这里，我们探索各种生物中同源蛋白的低聚状态，以更好地了解同源寡聚的功能作用和进化机制。我们观察到控制寡聚机制的多样性，我们的研究重点是同源蛋白质的插入和缺失以及它们如何启用或禁用复杂的形成。我们表明，区分单体和二聚体的插入和缺失具有位于相互作用界面上的显着趋势，并且大约所有研究的蛋白质的四分之一和40％的酶具有介导或破坏寡聚体形成的区域。我们建议相对较小的插入或缺失可能对复杂的稳定性和/或特异性产生深远的影响。实际上，在许多情况下，从蛋白质结构中去除复杂的使能区会导致稳定性的全部或部分丧失。此外，我们发现与常规界面和蛋白质表面相比，调节寡聚化的插入和缺失具有较低的聚集倾向，并且包含较大比例的极性，带电残基，甘氨酸和脯氨酸。这些区域很可能会介导特定的相互作用，防止非特异性的功能失调聚集，并阻止紧密旁系同源物之间的不良相互作用，从而分隔其功能途径。最后，我们展示了接口的插入或缺失的存在或缺失在注释蛋白寡聚态时如何具有实用价值。

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