Structural Requirements of a Glycolipid MPIase for Membrane Protein Integration
Structural Requirements of a Glycolipid MPIase for Membrane Protein Integration
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膜蛋白整合的糖脂 MPIase 的结构要求
DOI：
10.1002/chem.202300437
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发表时间：
2023
期刊：
影响因子：
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通讯作者：
Shimamoto Keiko
中科院分区：
文献类型：
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作者：
Fujikawa Kohki;Han Youjung;Osawa Tsukiho;Mori Shoko;Nomura Kaoru;Muramoto Maki;Nishiyama Ken‐ichi;Shimamoto Keiko
MPIase是一种参与大肠杆菌内膜膜蛋白整合的糖脂。为了克服天然MPIase的痕量和异质性，我们系统地合成了MPIase类似物。结构-活性关系研究揭示了不同官能团的贡献和mpase聚糖长度对膜蛋白整合活性的影响。此外，我们还观察了这些类似物与膜伴侣/插入酶YidC的协同作用，以及磷酸化聚糖的伴侣样活性。这些结果证实了e内膜中不依赖于转位的膜整合机制。在大肠杆菌中，MPIase通过其特有的官能团捕获高度疏水的新生蛋白，阻止蛋白质聚集，将蛋白质吸引到膜表面，并将其传递给YidC，以再生其自身的整合活性。
MPIase is a glycolipid involved in membrane protein integration in the inner membrane ofEscherichia coli. To overcome the trace amounts and heterogeneity of natural MPIase, we systematically synthesized MPIase analogs. Structure‐activity relationship studies revealed the contribution of distinctive functional groups and the effect of the MPIase glycan length on membrane protein integration activity. In addition, both the synergistic effects of these analogs with the membrane chaperone/insertase YidC, and the chaperone‐like activity of the phosphorylated glycan were observed. These results verified the translocon‐independent membrane integration mechanism in the inner membrane ofE. coli, in which MPIase captures the highly hydrophobic nascent proteins via its characteristic functional groups, prevents protein aggregation, attracts the proteins to the membrane surface, and delivers them to YidC in order to regenerate its own integration activity.