Phenotypes are established by tight regulation on protein functions. This regulation can be mediated allosterically, through protein binding, and covalently, through post-translational modification (PTM). The integration of an ever-increasing number of PTMs into regulatory networks enables and defines the proteome complexity. Protein PTMs can occur enzymatically and nonenzymatically. Polyphosphorylation, which is a recently discovered PTM that belongs to the latter category, is the covalent attachment of the linear ortho-phosphate polymer called inorganic polyphosphate (polyP) to lysine residues. PolyP, which is ubiquitously present in nature, is also known to allosterically control protein function. To date, lack of reagents has prevented the systematic analysis of proteins covalently and/or allosterically associated with polyP. Here, we report on the chemical synthesis of biotin-modified monodisperse short-chain polyP (bio-polyP8-bio) and its subsequent use to screen a human proteome array to identify proteins that associate with polyP, thereby starting to define the human polyP-ome.

中文翻译：

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用合成的生物素化的无机聚磷酸盐筛选蛋白质阵列，以定义人类PolyP-ome。

通过严格调节蛋白质功能来建立表型。此调节可通过蛋白结合和通过翻译后修饰（PTM）共价来进行变构介导。将越来越多的PTM集成到监管网络中，可以定义蛋白质组的复杂性。蛋白质PTM可以通过酶和非酶方式发生。多磷酸化是最近发现的属于后者的PTM，是线性邻位的共价结合磷酸酯称为无机多磷酸酯（polyP）的赖氨酸残基。众所周知，自然界普遍存在的PolyP可以变构地控制蛋白质功能。迄今为止，缺乏试剂已经阻止了与polyP共价和/或变构结合的蛋白质的系统分析。在这里，我们报告了生物素修饰的单分散短链polyP（bio-polyP8-bio）的化学合成及其随后用于筛选人类蛋白质组阵列以鉴定与polyP相关的蛋白质，从而开始定义人类polyP-来吧