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PspA采用类似于ESCRT-III的折叠方式,重塑细菌膜

Benedikt Junglas¹, Stefan T Huber², Thomas Heidler³

¹Ernst-Ruska Centre for Microscopy and Spectroscopy with Electrons, ER-C-3/Structural Biology, Forschungszentrum Jülich, 52425 Jülich, Germany; JuStruct: Jülich Center for Structural Biology, Forschungszentrum Jülich, 52425 Jülich, Germany; Department of Chemistry, Biochemistry, Johannes Gutenberg University Mainz, 55128 Mainz, Germany.

|June 24, 2021

概括

细菌PspA蛋白对于内膜的完整性至关重要, 形成螺旋杆, 重塑膜. 这些结构包围脂质,产生曲率,并调解囊泡形成,连接脂质结构.

科学领域:

微生物学
结构生物学
生物化学

背景情况:

菌体冲击蛋白 (Psp) 系统对于细菌在压力下生存至关重要.
PspA是PSP系统的主要效应蛋白,维护细菌内膜的完整性和功能.
细菌PspA与参与膜重塑的ESCRT-III蛋白质具有同质性.

研究的目的:

确定组装成螺旋杆的PSPA的高分辨率结构.
阐明PSPA重塑细菌膜的机制.
了解PSPA和ESCRT-III蛋白之间的进化关系.

主要方法:

使用3.6 Å分辨率的冷电子显微镜 (cryo-EM) 来确定PSPA组件的结构.
用功能测试观察PspA在体外的膜重塑能力.
进行了比较结构分析,以将PspA与ESCRT-III蛋白联系起来.

主要成果:

冷-EM结构显示了具有ESCRT-III折叠的扩展开放形状的PSPA单体.
观察到PSPA螺旋棒包围脂质,产生正面膜曲率,并重塑膜囊泡.
PspA组件作为脂质转移的平台,连接单独的脂质结构并调解膜融合和裂变.

结论:

细菌PspA形成具有ESCRT-III折叠的螺旋杆,使其能够进行显著的膜重塑活动.
PspA封闭脂质,产生曲和调节囊泡形成的能力对于细菌膜平衡至关重要.
PspA代表ESCRT-III蛋白家族的古老成员,突出显示了在整个进化过程中膜重塑的保存机制.

关键词:

欧洲权益与发展委员会-III IM30 其他美国一个Vipp1 化电磁场化ET 螺旋式重建膜裂变膜融合膜改造膜管道

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