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Resilin matrix distribution, variability and function in Drosophila
BMC Biology ( IF 4.4 ) Pub Date : 2020-12-14 , DOI: 10.1186/s12915-020-00902-4
Steven Lerch 1, 2, 3 , Renata Zuber 1 , Nicole Gehring 2 , Yiwen Wang 2 , Barbara Eckel 1 , Klaus-Dieter Klass 3 , Fritz-Olaf Lehmann 4 , Bernard Moussian 1, 2, 5
Affiliation  

Elasticity prevents fatigue of tissues that are extensively and repeatedly deformed. Resilin is a resilient and elastic extracellular protein matrix in joints and hinges of insects. For its mechanical properties, Resilin is extensively analysed and applied in biomaterial and biomedical sciences. However, there is only indirect evidence for Resilin distribution and function in an insect. Commonly, the presence of dityrosines that covalently link Resilin protein monomers (Pro-Resilin), which are responsible for its mechanical properties and fluoresce upon UV excitation, has been considered to reflect Resilin incidence. Using a GFP-tagged Resilin version, we directly identify Resilin in pliable regions of the Drosophila body, some of which were not described before. Interestingly, the amounts of dityrosines are not proportional to the amounts of Resilin in different areas of the fly body, arguing that the mechanical properties of Resilin matrices vary according to their need. For a functional analysis of Resilin matrices, applying the RNA interference and Crispr/Cas9 techniques, we generated flies with reduced or eliminated Resilin function, respectively. We find that these flies are flightless but capable of locomotion and viable suggesting that other proteins may partially compensate for Resilin function. Indeed, localizations of the potentially elastic protein Cpr56F and Resilin occasionally coincide. Thus, Resilin-matrices are composite in the way that varying amounts of different elastic proteins and dityrosinylation define material properties. Understanding the biology of Resilin will have an impact on Resilin-based biomaterial and biomedical sciences.

中文翻译:

果蝇中的弹性蛋白基质分布、变异性和功能

弹性可防止广泛且反复变形的组织疲劳。Resilin 是昆虫关节和铰链中的一种有弹性和弹性的细胞外蛋白质基质。由于其机械性能,Resilin 在生物材料和生物医学科学中被广泛分析和应用。然而,只有间接证据表明 Resilin 在昆虫中的分布和功能。通常,存在共价连接 Resilin 蛋白单体 (Pro-Resilin) 的二酪氨酸被认为反映了 Resilin 的发生率。使用 GFP 标记的 Resilin 版本,我们直接在果蝇身体的柔韧区域中识别 Resilin,其中一些以前没有描述过。有趣的是,二酪氨酸的数量与苍蝇身体不同区域的 Resilin 数量不成正比,认为 Resilin 基质的机械性能根据需要而变化。对于 Resilin 矩阵的功能分析,应用 RNA 干扰和 Crispr/Cas9 技术,我们分别生成了 Resilin 功能减少或消除的果蝇。我们发现这些果蝇不会飞,但能够运动且可行,这表明其他蛋白质可能会部分补偿 Resilin 功能。事实上,潜在弹性蛋白 Cpr56F 和 Resilin 的定位偶尔会重合。因此,Resilin 基质是以不同数量的不同弹性蛋白和二酪氨酸化定义材料特性的方式复合的。
更新日期:2020-12-15
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