酵母菌中磷脂醯肌醇-5-磷酸结合蛋白相互作用的系统分析對真核生物具有很高的生物學意義。在這裡，我們使用酵母蛋白體微陣列（〜5800個纯化的蛋白質）對PI5P结合蛋白進行了高通量和系统的篩選。根據探测含PI5P的螢光奈米脂粒於酵母蛋白體晶片及使用流式细胞儀驗證，總共鑑定出41個PI5P结合蛋白。富集分析揭示了與核糖體合成和rRNA加工相關的重要功能。蛋白質的位置富集於核酸，分子功能方面富集於水解酶活性。 InterPro域分析表明，PI5P结合蛋白富集於P環。此外，使用MEME，我們進一步確定了一組共有基序（IVGPAGTGKSTLF），該基序包含Walker A序列，即眾所周知的核苷酸結合基序。此外，使用石英晶體微量天平，共有基序和Walker A基序均顯示出與含PI5P的脂質體有强结合，而與不含PI5P的脂質體和含PI的脂質體無结合。這項研究不僅確定了一组新的PI5P结合蛋白，而且還揭示了Walker A基序具有很强的PI5P结合力（Kd = 1.81 x 10-7 M）。本研究拓寬PI5P 結合酵母菌蛋白的範疇並提出PI5P在酵母模型系統中潛在功能的新見解。

Systematic analysis of phosphatidylinositol-5-phosphate (PI5P)-binding protein interactome in the yeast system holds a high biological significance for eukaryotes. Here, we used yeast proteome microarrays (~5800 purified proteins) to conduct a high-throughput and systematic screening of PI5P-binding proteins. Based on probing the PI5P-containing fluorescent liposomal nanovesicles to the yeast proteome chip, and subsequently using flow cytometry to validate, a total of 41 PI5P-binding proteins were identified. Enrichment analysis revealed significant functions associated with ribosome biogenesis and rRNA-processing. Nucleolus and hydrolase activity were enriched in terms of proteins’ location and molecular function, respectively. The InterPro domain analysis indicated that PI5P-binding proteins are enriched in P-loop containing nucleoside triphosphate hydrolases domain (P-loop). Using the MEME program, we further identified a consensus motif (IVGPAGTGKSTLF) which contains Walker A sequence, a well-known nucleotide-binding motif. Using quartz crystal microbalance (QCM), both the consensus motif and Walker A motif also showed strong binding to PI5P-containing liposomes, but not PI5P-deprived liposomes and PI-containing liposomes. This study not only identified a new set of PI5P-binding proteins but also revealed the strong PI5P-binding affinity (Kd = 1.81 x 10-7 M) of Walker A motif. The current study widens the spectrum of PI5P-binding yeast proteins and opens the new insight related to the potential functionality of PI5P in the yeast model system.

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