Dual function of OmpM as outer membrane tether and nutrient uptake channel in diderm Firmicutes
Augustinas Silale,
Yiling Zhu,
Jerzy Witwinowski,
Robert E. Smith,
Kahlan E. Newman,
Satya P. Bhamidimarri,
Arnaud Baslé,
Syma Khalid,
Christophe Beloin (),
Simonetta Gribaldo () and
Bert Berg ()
Additional contact information
Augustinas Silale: Newcastle University, Framlington Place
Yiling Zhu: Newcastle University, Framlington Place
Jerzy Witwinowski: Unit Evolutionary Biology of the Microbial Cell
Robert E. Smith: Unit Evolutionary Biology of the Microbial Cell
Kahlan E. Newman: University of Southampton
Satya P. Bhamidimarri: Newcastle University, Framlington Place
Arnaud Baslé: Newcastle University, Framlington Place
Syma Khalid: University of Oxford
Christophe Beloin: Genetics of Biofilms Laboratory
Simonetta Gribaldo: Unit Evolutionary Biology of the Microbial Cell
Bert Berg: Newcastle University, Framlington Place
Nature Communications, 2023, vol. 14, issue 1, 1-18
Abstract:
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.
Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-42601-y
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DOI: 10.1038/s41467-023-42601-y
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