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具有 BAR 结构域样活性的细菌膜成型蛋白。

A bacterial membrane sculpting protein with BAR domain-like activity.

机构信息

U.S. Army DEVCOM Chemical Biological Center, BioSciences Division, BioChemistry Branch, Aberdeen Proving Ground, United States.

Oak Ridge Institute for Science and Education, Oak Ridge, United States.

出版信息

Elife. 2021 Oct 13;10:e60049. doi: 10.7554/eLife.60049.

DOI:10.7554/eLife.60049
PMID:34643180
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8687657/
Abstract

Bin/Amphiphysin/RVS (BAR) domain proteins belong to a superfamily of coiled-coil proteins influencing membrane curvature in eukaryotes and are associated with vesicle biogenesis, vesicle-mediated protein trafficking, and intracellular signaling. Here, we report a bacterial protein with BAR domain-like activity, BdpA, from MR-1, known to produce redox-active membrane vesicles and micrometer-scale outer membrane extensions (OMEs). BdpA is required for uniform size distribution of membrane vesicles and influences scaffolding of OMEs into a consistent diameter and curvature. Cryo-TEM reveals that a strain lacking BdpA produces lobed, disordered OMEs rather than membrane tubules or narrow chains produced by the wild-type strain. Overexpression of BdpA promotes OME formation during planktonic growth of where they are not typically observed. Heterologous expression results in OME production in and . Based on the ability of BdpA to alter membrane architecture in vivo, we propose that BdpA and its homologs comprise a newly identified class of bacterial BAR domain-like proteins.

摘要

Bin/Amphiphysin/RVS (BAR) 结构域蛋白属于卷曲螺旋蛋白超家族，影响真核生物的膜曲率，与囊泡发生、囊泡介导的蛋白质运输和细胞内信号转导有关。在这里，我们报告了一种来自 MR-1 的具有 BAR 结构域样活性的细菌蛋白 BdpA，MR-1 已知会产生氧化还原活性的膜囊泡和微米尺度的外膜延伸（OME）。BdpA 是膜囊泡大小均匀分布所必需的，并影响 OME 成束到一致的直径和曲率。低温透射电镜显示，缺乏 BdpA 的菌株产生的是有叶的、无序的 OME，而不是野生型菌株产生的管状或窄链状囊泡。BdpA 的过表达促进了浮游生长过程中 OME 的形成，而在浮游生长中通常不会观察到 OME。异源表达导致 和 中产生 OME。基于 BdpA 在体内改变膜结构的能力，我们提出 BdpA 及其同源物构成了一个新发现的细菌 BAR 结构域样蛋白家族。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/031f/8687657/91bbbc9cbc72/elife-60049-fig5-figsupp1.jpg
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