Sequential Translocation of Polypeptides across the Bacterial Outer Membrane through the Trimeric Autotransporter Pathway.
Bam complex
membrane proteins
outer membrane
protein folding
protein secretion
trimeric autotransporters
Journal
mBio
ISSN: 2150-7511
Titre abrégé: mBio
Pays: United States
ID NLM: 101519231
Informations de publication
Date de publication:
22 10 2019
22 10 2019
Historique:
entrez:
24
10
2019
pubmed:
24
10
2019
medline:
19
5
2020
Statut:
epublish
Résumé
Trimeric autotransporter adhesins (TAAs) are a family of bacterial outer membrane (OM) proteins that are comprised of three identical subunits. Each subunit contains an N-terminal extracellular ("passenger") domain and a short C-terminal segment that contributes four β strands to a single 12-stranded β barrel. The mechanism by which the passenger domains are translocated across the OM and the energetics of the translocation reaction are poorly understood. To address these issues, we examined the secretion of modified versions of the passenger domain of UpaG, a TAA produced by
Identifiants
pubmed: 31641085
pii: mBio.01973-19
doi: 10.1128/mBio.01973-19
pmc: PMC6805991
pii:
doi:
Substances chimiques
Bacterial Outer Membrane Proteins
0
Membrane Proteins
0
Peptides
0
Types de publication
Journal Article
Research Support, N.I.H., Intramural
Langues
eng
Sous-ensembles de citation
IM
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