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首页> 外文期刊>Proceedings of the National Academy of Sciences of the United States of America >Molecular basis of coiled-coil oligomerization-state specificity
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Molecular basis of coiled-coil oligomerization-state specificity

机译：卷曲螺旋低聚态特异性的分子基础

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摘要

Coiled coils are extensively and successfully used nowadays to rationally design multistranded structures for applications, including basic research, biotechnology, nanotechnology, materials science, and medicine. The wide range of applications as well as the important functions these structures play in almost all biological processes highlight the need for a detailed understanding of the factors that control coiled-coil folding and oligomerization. Here, we address the important and unresolved question why the presence of particular oligomerization-state determinants within a coiled coil does frequently not correlate with its topology. We found an unexpected, general link between coiled-coil oligomerization-state specificity and trigger sequences, elements that are indispensable for coiled-coil formation. By using the archetype coiled-coil domain of the yeast transcriptional activator GCN4 as a model system, we show that well-established trimer-specific oligomerization-state determinants switch the peptide's topology from a dimer to a trimer only when inserted into the trigger sequence. We successfully confirmed our results in two other, unrelated coiled-coil dimers, ATF1 and cortexillin-1. We furthermore show that multiple topology determinants can coexist in the same trigger sequence, revealing a delicate balance of the resulting oligomerization state by position-dependent forces. Our experimental results should significantly improve the prediction of the oligomerization state of coiled coils. They therefore should have major implications for the rational design of coiled coils and consequently many applications using these popular oligomerization domains.
机译：如今，盘绕线圈已广泛且成功地用于合理设计用于应用的多股结构，包括基础研究，生物技术，纳米技术，材料科学和医学。这些结构在几乎所有生物过程中的广泛应用以及重要功能，凸显了需要详细了解控制卷曲螺旋折叠和低聚的因素。在这里，我们解决了一个重要且尚未解决的问题，即为什么在盘绕的卷材中特定低聚状态决定簇的存在通常与其拓扑不相关。我们发现，卷曲螺旋低聚态特异性与触发序列之间有一个出乎意料的一般联系，而触发序列是卷曲螺旋形成必不可少的元素。通过使用酵母转录激活因子GCN4的原型卷曲螺旋结构域作为模型系统，我们证明了公认的三聚体特异性寡聚化状态决定簇仅在插入触发序列时才将肽的拓扑结构从二聚体切换为三聚体。我们在另外两个无关的卷曲螺旋二聚体ATF1和cortexillin-1中成功证实了我们的结果。我们进一步表明，多个拓扑决定因素可以在同一触发序列中共存，通过位置相关的力揭示了所得寡聚态的微妙平衡。我们的实验结果应大大改善对卷曲卷材低聚状态的预测。因此，它们应该对线圈的合理设计产生重大影响，并因此对使用这些流行的低聚结构域的许多应用产生重大影响。

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    Barbara Ciani; Sasa Bjelic; Srinivas Honnappa; Hatim Jawhari; Rolf Jaussi; Aishwarya Payapilly; Thomas Jowitt; Michel O. Steinmetz; Richard A. Kammerer;

  • 作者单位

    Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom,Department of Chemistry, University of Sheffield, Sheffield S3 7HF, United Kingdom;

    Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland;

    Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland,Novartis Institutes for Biomedical Research, Novartis Pharma AG, 4002, Basel, Switzerland;

    Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland,Roche Applied Science Customer Support Centre, Roche Diagnostics GmbH, D-68305 Mannheim, Germany;

    Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland;

    Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom;

    Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom;

    Biomolecular Research, Paul Scherrer Institut, CH-5232 Villigen PSI, Switzerland;

    Wellcome Trust Centre for Cell-Matrix Research, Faculty of Life Sciences, University of Manchester, Manchester M13 9PT, United Kingdom,Biomolecular Research, Paul Scherrer Insititut, CH-5232 Villigen PSI, Switzerland;

  • 收录信息 美国《科学引文索引》(SCI);美国《生物学医学文摘》(MEDLINE);美国《化学文摘》(CA);
  • 原文格式 PDF
  • 正文语种 eng
  • 中图分类
  • 关键词

    protein folding; protein structure; protein-protein interactions;

    机译：蛋白质折叠蛋白质结构;蛋白质相互作用;

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