Dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes
Year: 2023
Type: article
Abstract: The outer membrane (OM) in diderm, or Gram-negative, bacteria must be tethered to peptidoglycan for mechanical stability and to maintain cell morphology. Most diderm phyla from the Terrabacteria group have recently been shown to lack well-characterised OM attachment systems, but instead have OmpM, which could represent an ancestral tethering system in bacteria. Here, we have determined the structure of the most abundant OmpM protein from Veillonella parvula (diderm Firmicutes) by single particle cryogenic electron microscopy. We also characterised the channel properties of the transmembrane β-barrel of OmpM and investigated the structure and PG-binding properties of its periplasmic stalk region. Our results show that OM tethering and nutrient acquisition are genetically linked in V. parvula , and probably other diderm Terrabacteria. This dual function of OmpM may have played a role in the loss of the OM in ancestral bacteria and the emergence of monoderm bacterial lineages.
Source: Nature Communications
Language: English
Subfield: Genetics
Domain: Life Sciences
Open Access status: gold
Estimated APC paid: $3,031
Awards: Firmicutes with an outer membrane: toward new models to study the diderm/monoderm cell envelope transition, G1979782309, Identifying the Molecular Determinants of Ferredoxin Transport into the Periplasm of Pectobacterium spp., Understanding small molecule uptake by the Bacteroidetes, G282427092, G2995304911, G3256177976, G4986318432, G5420063140, Understanding small molecule uptake by the Bacteroidetes, G693515516, G7240651115, G7376787254, G7428494302, Integrative Biology of Emerging Infectious Diseases, G7706394089, MOLSImage: Combining Simulations and Imaging to Deliver Next Generation Tools for Studying Bacterial Cell Envelopes., G8670608220
OpenAlex ID: W4388407503