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A photostable monomeric superfolder green fluorescent protein.
Traffic ( IF 3.6 ) Pub Date : 2020-05-15 , DOI: 10.1111/tra.12737
Fernando M Valbuena 1 , Ivy Fitzgerald 2 , Rita L Strack 1 , Neal Andruska 1 , Luke Smith 1 , Benjamin S Glick 1
Affiliation  

The green fluorescent protein (GFP) from Aequorea victoria has been engineered extensively in the past to generate variants suitable for protein tagging. Early efforts produced the enhanced variant EGFP and its monomeric derivative mEGFP, which have useful photophysical properties, as well as superfolder GFP, which folds efficiently under adverse conditions. We previously generated msGFP, a monomeric superfolder derivative of EGFP. Unfortunately, compared to EGFP, msGFP and other superfolder GFP variants show faster photobleaching. We now describe msGFP2, which retains monomeric superfolder properties while being as photostable as EGFP. msGFP2 contains modified N‐ and C‐terminal peptides that are expected to reduce nonspecific interactions. Compared to EGFP and mEGFP, msGFP2 is less prone to disturbing the functions of certain partner proteins. For general‐purpose protein tagging, msGFP2 may be the best available derivative of A. victoria GFP.

中文翻译:

一种光稳定的单体超级折叠绿色荧光蛋白。

来自维多利亚水母的绿色荧光蛋白 (GFP)过去已被广泛设计以生成适合蛋白质标记的变体。早期的努力产生了增强的变体 EGFP 及其单体衍生物 mEGFP,它们具有有用的光物理特性,以及在不利条件下有效折叠的超级文件夹 GFP。我们之前生成了 msGFP,这是 EGFP 的单体超文件夹衍生物。不幸的是,与 EGFP 相比,msGFP 和其他超级文件夹 GFP 变体显示出更快的光漂白。我们现在描述 msGFP2,它保留了单体超级文件夹属性,同时与 EGFP 一样耐光。msGFP2 包含修饰的 N 和 C 端肽,预计可减少非特异性相互作用。与 EGFP 和 mEGFP 相比,msGFP2 不太容易干扰某些伙伴蛋白的功能。对于通用蛋白质标记,A. 维多利亚GFP。
更新日期:2020-07-22
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