RT Journal Article
SR Electronic
T1 A Prokaryotic Membrane Sculpting BAR Domain Protein
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2020.01.30.926147
DO 10.1101/2020.01.30.926147
A1 Daniel A. Phillips
A1 Lori A. Zacharoff
A1 Cheri M. Hampton
A1 Grace W. Chong
A1 Anthony P. Malanoski
A1 Lauren Ann Metskas
A1 Shuai Xu
A1 Lina J. Bird
A1 Brian J. Eddie
A1 Grant J. Jensen
A1 Lawrence F. Drummy
A1 Mohamed Y. El-Naggar
A1 Sarah M. Glaven
YR 2020
UL http://biorxiv.org/content/early/2020/01/31/2020.01.30.926147.abstract
AB Bin/Amphiphysin/RVS (BAR) domain proteins belong to a ubiquitous superfamily of coiled-coil proteins that influence membrane curvature in eukaryotes and are associated with vesicle biogenesis, vesicle-mediated protein trafficking, and intracellular signaling1–6. BAR domain proteins have not been identified in bacteria, despite certain organisms displaying an array of membrane curvature phenotypes7–16. Here we identify a prokaryotic BAR domain protein, BdpA, from Shewanella oneidensis MR-1, an iron reducing bacterium known to produce redox active membrane vesicles and micrometer-scale membrane extensions. BdpA is required for uniform size distribution of outer membrane vesicles and is responsible for scaffolding outer membrane extensions (OMEs) into membrane structures with consistent diameter and curvature. While a strain lacking BdpA produces OMEs, cryogenic transmission electron microscopy reveals more lobed, disordered OMEs rather than the membrane tubes produced by the wild type strain. Overexpression of BdpA promotes OME formation even during planktonic conditions where S. oneidensis OMEs are less common. Heterologous expression also results in OME production in Marinobacter atlanticus CP1 and Escherichia coli. Based on the ability of BdpA to alter membrane curvature in vivo, we propose that BdpA and its homologs comprise a newly identified class of prokaryotic BAR (P-BAR) domains that will aid in identification of putative P-BAR proteins in other bacterial species.