使用 NanoBiT 分析 UDP-半乳糖转运蛋白与β-1,4-半乳糖基转移酶 1 之间的同源和异源相互作用。
Analysis of homologous and heterologous interactions between UDP-galactose transporter and beta-1,4-galactosyltransferase 1 using NanoBiT.
机构信息
Laboratory of Biochemistry, Faculty of Biotechnology, University of Wroclaw, 14A F. Joliot-Curie St., 50-383, Wroclaw, Poland.
Human Genetics Program, Sanford Burnham Prebys Medical Discovery Institute, La Jolla, CA, USA.
出版信息
Anal Biochem. 2020 Mar 15;593:113599. doi: 10.1016/j.ab.2020.113599. Epub 2020 Jan 28.
Split luciferase complementation assay is one of the approaches enabling identification and analysis of protein-protein interactions in vivo. The NanoBiT technology is the most recent improvement of this strategy. Nucleotide sugar transporters and glycosyltransferases of the Golgi apparatus are the key players in glycosylation. Here we demonstrate the applicability of the NanoBiT system for studying homooligomerization of these proteins. We also report and discuss a novel heterologous interaction between UDP-galactose transporter and beta-1,4-galactosyltransferase 1.
Split luciferase complementation assay 是一种能够在体内鉴定和分析蛋白质-蛋白质相互作用的方法。NanoBiT 技术是该策略的最新改进。核苷酸糖转运蛋白和高尔基体内的糖基转移酶是糖基化的关键因素。在这里，我们展示了 NanoBiT 系统在研究这些蛋白质同源寡聚化中的适用性。我们还报告并讨论了 UDP-半乳糖转运蛋白和β-1,4-半乳糖基转移酶 1 之间新的异源相互作用。
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