A bacterial membrane sculpting protein with BAR domain-like activity

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-li...

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Published in:eLife 2021-10, Vol.10
Main Authors: Phillips, Daniel A., Zacharoff, Lori A., Hampton, Cheri M., Chong, Grace W., Malanoski, Anthony P., Metskas, Lauren Ann, Xu, Shuai, Bird, Lina J., Eddie, Brian J., Miklos, Aleksandr E., Jensen, Grant J., Drummy, Lawrence F., El-Naggar, Mohamed Y., Glaven, Sarah M.
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Language:English
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Life Sciences & Biomedicine - Other Topics
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Summary: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, fromShewanella oneidensisMR-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 ofS. oneidensiswhere they are not typically observed. Heterologous expression results in OME production inMarinobacter atlanticusandEscherichia 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.
ISSN:2050-084X
2050-084X
DOI:10.7554/eLife.60049