Details

Autor(en) / Beteiligte

• 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

Titel

A bacterial membrane sculpting protein with BAR domain-like activity

Ist Teil von

• eLife, 2021-10, Vol.10

Ort / Verlag

England: eLife Sciences Publications Ltd

Erscheinungsjahr

2021

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.