A bacterial membrane sculpting protein with BAR domain-like activity

eLife

Grant J Jensen¹  Sarah M Glaven²  Anthony P Malanoski²  Lina J Bird²  Brian J Eddie²  Lawrence F Drummy³  Cheri M Hampton³  Aleksandr E Miklos⁴  Lauren Ann Metskas⁴  Daniel A Phillips⁵  Grace W Chong⁶  Mohamed Y El-Naggar⁷  Shuai Xu⁸  Lori A Zacharoff⁸ 

[1]California Institute of Technology, Division of Biology and Biological Engineering, Pasadena, United States

[2]Department of Chemistry and Biochemistry, Brigham Young University, Provo, United States

[3]Center for Bio/Molecular Science and Engineering, Naval Research Laboratory, Washington, United States

[4]Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Dayton, United States

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

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

[7]Oak Ridge Institute for Science and Education, Oak Ridge, United States

[8]University of Southern California, Department of Biological Sciences, Los Angeles, United States

[9]University of Southern California, Department of Chemistry, Los Angeles, United States

[10]University of Southern California, Department of Physics and Astronomy, Los Angeles, United States

关键词: BAR domain;    extracellular electron transport;    membrane shaping;    outer membrane vesicles;    outer membrane extensions;    Shewanella;    E. coli;    Other;   

DOI  :  10.7554/eLife.60049

来源: eLife Sciences Publications, Ltd

【 摘 要 】

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 Shewanella oneidensis 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 S. oneidensis where they are not typically observed. Heterologous expression results in OME production in Marinobacter atlanticus and Escherichia coli. 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.

【 授权许可】

CC BY