The IM30/Vipp1 C-terminus associates with the lipid bilayer and modulates membrane fusion

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• 作者：Raoul Hennig^a ; Ana West^b ; Martina Debus^a ; Michael Saur^c ; Jü ; rgen Markl^c ; Jonathan N. Sachs^b ; Dirk Schneider^a ; ^{Dirk.Schneider@uni-mainz.de}
• 关键词：Vipp1 ; PspA ; Thylakoid membrane ; Membrane biogenesis ; Membrane fusion
• 刊名：Biochimica et Biophysica Acta (BBA) - Bioenergetics
• 出版年：2017
• 出版时间：February 2017
• 年：2017
• 卷：1858
• 期：2
• 页码：126-136
• 全文大小：1306 K
• 卷排序：1858

文摘

The IM30 C-terminus does not affect the structure and stability of IM30. Membrane binding of IM30 involves the PspA- as well as the C-terminal domain. The IM30 C-terminus interacts with negatively charged membrane surfaces. Charged residues inside the IM30 C-terminus influence stability of membrane binding. Membrane binding of the IM30 C-terminus correlates with the proteins fusogenic activity.