蜘蛛丝的翻译后修饰影响构象和二聚化动力学

IF 4.1 3区 材料科学 Q2 MATERIALS SCIENCE, MULTIDISCIPLINARY
H. C. Craig, A. D. Malay, F. Hayashi, M. Mori, K. Arakawa, K. Numata
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引用次数: 0

摘要

摘要蜘蛛丝是一种典型的生物聚合物材料,由于其复杂的分层组装而具有极强的拉伸性能。虽然近年来测序技术的进步带来了丰富的研究成果,但人们对蜘蛛丝翻译后修饰(PTM)的了解却相对较少。在这里,我们采用质谱和固态核磁共振(NMR)相结合的方法,探究了Jorō蜘蛛(Trichonephila clavata)拖丝的PTM结构。结果发现了一系列潜在的修饰,包括羟脯氨酸、磷酸化和酪氨酸交联,涵盖了不同的蜘蛛素成分。值得注意的是,MaSp3的重复区域显示了许多PTM,而MaSp1和MaSp2变体的末端结构域则显示了不同的磷酸化模式。N 端结构域(NTD)的磷酸化位点主要出现在二聚体界面上,这表明它对 pH 驱动的二聚化功能具有调节作用,利用磷酸拟态 NTD 突变体进行的研究支持了这一假设。此外,还讨论了膦丝氨酸在限制 β 片层形成方面的可能作用,以及羟脯氨酸在破坏 β 转折方面的可能作用。影响声明蜘蛛丝是一种典型的生物材料,其性能超过了我们最复杂的人造纤维。其机械性能的秘密在于其复杂的分层结构--从纳米到宏观--是通过组成蛛丝蛋白的分子自组装过程形成的。虽然 "生物材料组学 "的最新进展让我们对决定蛛丝行为的序列-功能关系有了更深入的了解,但这幅图景还远远不够完整。翻译后修饰(PTMs)是一个很少受到关注的领域。PTMs 是一种无处不在的生物现象,对蛋白质组的动态控制至关重要,它有效地扩展了蛋白质的结构和功能设计空间,使其超越了典型氨基酸所提供的空间。在这里,我们对蜘蛛拖丝纤维中的 PTMs 进行了全面分析,发现了大量潜在的修饰位点。这些结果为了解蜘蛛丝机械行为背后更多层次的复杂性提供了一个令人着迷的窗口,并为创造新颖、动态可调的生物启发材料提供了更多途径。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Posttranslational modifications in spider silk influence conformation and dimerization dynamics

Posttranslational modifications in spider silk influence conformation and dimerization dynamics

Abstract

Spider silk is an archetypal biopolymer material with extreme tensile properties arising from its complex hierarchical assembly. While recent advances in sequencing have yielded abundant insights, relatively little is known concerning post-translational modifications (PTMs) in spider silk. Here, we probe the PTM landscape of dragline silk from the Jorō spider (Trichonephila clavata) using a combination of mass spectroscopy and solid-state nuclear magnetic resonance (NMR). The results reveal a wide array of potential modifications, including hydroxyproline, phosphorylation, and dityrosine cross-links, encompassing the different spidroin constituents. Notably, the MaSp3 repetitive region displayed numerous PTMs, whereas MaSp1 and MaSp2 variants showed distinct phosphorylation patterns in its terminal domains. The N-terminal domain (NTD) phosphorylation sites were found predominantly at the dimer interface, suggesting a modulatory function with respect to its pH-driven dimerization function, a hypothesis supported by studies using phosphomimetic NTD mutants. Possible roles of phosphoserine in limiting β-sheet formation, and hydroxyproline in disrupting β-turns are also discussed.

Impact statement

Spider silk is an archetypal biomaterial that can outperform our most sophisticated artificial fibers. The secret to its mechanical properties lies in its complex hierarchical structure—encompassing the nano- to macroscales—that forms through a process of molecular self-assembly of the constituent spidroin proteins. While recent advances in "biomateriomics” have given us tremendous insights into the sequence–function relationships that determine spider silk behavior, the picture is still far from complete. One area that has received little attention is posttranslational modifications (PTMs). PTMs are ubiquitous biological phenomena that are crucial for providing dynamic control of the proteome, and effectively expand the structural and functional design space of proteins beyond that provided by the canonical amino acids. Here, we undertook a comprehensive analysis of PTMs from spider dragline silk fiber, which revealed numerous potential sites for a wide array of modifications. The results provide a fascinating window into additional layers of complexity underlying the mechanical behavior of spider silk, and suggest further avenues for creating novel, dynamically tunable, bioinspired materials.

Graphical abstract

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来源期刊
Mrs Bulletin
Mrs Bulletin 工程技术-材料科学:综合
CiteScore
7.40
自引率
2.00%
发文量
193
审稿时长
4-8 weeks
期刊介绍: MRS Bulletin is one of the most widely recognized and highly respected publications in advanced materials research. Each month, the Bulletin provides a comprehensive overview of a specific materials theme, along with industry and policy developments, and MRS and materials-community news and events. Written by leading experts, the overview articles are useful references for specialists, but are also presented at a level understandable to a broad scientific audience.
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