Structure and function of PspA and Vipp1 N-terminal peptides: Insights into the membrane stress sensing and mitigation

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• 作者：Christopher McDonald^a ; ^b ; Goran Jovanovic^a ; B.A. Wallace^c ; Oscar Ces^b ; Martin Buck^a ; ^{m.buck@imperial.ac.uk}
• 关键词：Psp ; Phage shock protein ; pmf ; proton motive force ; IM ; inner membrane ; TLE ; total lipid extract ; PG ; phosphatidylglycerol ; PS ; phosphatidylserine ; SCE ; stored curvature elastic ; AH ; amphipathic helix ; ITC ; isothermal titration calorimetry ; CD ; circular dichroism ; SUV ; small unilamellar vesicle ; DOPC ; 1 ; 2-dioleoyl-sn-glycero-3-phosphocholine ; DOPG ; 1 ; 2-dioleoyl-sn-glycero-3-phospho-(1&prime ; -rac-glycerol) ; LUV ; large unilamellar vesicle ; DMPC ; 1 ; 2-dimyristoyl-sn-glycero-3-phosphocholine ; DOPE ; 1
• 刊名：Biochimica et Biophysica Acta (BBA) - Biomembranes
• 出版年：2017
• 出版时间：January 2017
• 年：2017
• 卷：1859
• 期：1
• 页码：28-39
• 全文大小：1734 K
• 卷排序：1859

文摘

PspA and Vipp1 require their N-terminal amphipathic helix a (AHa) to bind lipid vesicles. The AHa undergoes an unordered to α-helical transition upon membrane association. The AHa directly sense membrane stored curvature elastic stress and anionic lipids. The AHa can change bilayer stability. Use of AHa allows PspA to switch from its regulatory to an effector function.