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Nature (London), 2023-01, Vol.613 (7945), p.729-734
2023

Details

Autor(en) / Beteiligte
Titel
Two broadly conserved families of polyprenyl-phosphate transporters
Ist Teil von
  • Nature (London), 2023-01, Vol.613 (7945), p.729-734
Ort / Verlag
England: Nature Publishing Group
Erscheinungsjahr
2023
Link zum Volltext
Quelle
MEDLINE
Beschreibungen/Notizen
  • Peptidoglycan and almost all surface glycopolymers in bacteria are built in the cytoplasm on the lipid carrier undecaprenyl phosphate (UndP) . These UndP-linked precursors are transported across the membrane and polymerized or directly transferred to surface polymers, lipids or proteins. UndP is then flipped to regenerate the pool of cytoplasmic-facing UndP. The identity of the flippase that catalyses transport has remained unknown. Here, using the antibiotic amphomycin that targets UndP , we identified two broadly conserved protein families that affect UndP recycling. One (UptA) is a member of the DedA superfamily ; the other (PopT) contains the domain DUF368. Genetic, cytological and syntenic analyses indicate that these proteins are UndP transporters. Notably, homologues from Gram-positive and Gram-negative bacteria promote UndP transport in Bacillus subtilis, indicating that recycling activity is broadly conserved among family members. Inhibitors of these flippases could potentiate the activity of antibiotics targeting the cell envelope.

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