The structure and mechanism of the bacterial type II secretion system.
Amino Acid Sequence
Animals
Bacterial Outer Membrane Proteins
/ chemistry
Bacterial Physiological Phenomena
Bacterial Proteins
/ chemistry
Cryoelectron Microscopy
Fimbriae, Bacterial
/ chemistry
Humans
Models, Molecular
Protein Conformation
Secretin
/ metabolism
Type II Secretion Systems
/ chemistry
Virulence Factors
/ chemistry
assembly platform
cryo-EM
secretin
structure
type II secretion system
type IV pilus system
Journal
Molecular microbiology
ISSN: 1365-2958
Titre abrégé: Mol Microbiol
Pays: England
ID NLM: 8712028
Informations de publication
Date de publication:
03 2021
03 2021
Historique:
revised:
03
12
2020
received:
01
09
2020
pubmed:
8
12
2020
medline:
28
9
2021
entrez:
7
12
2020
Statut:
ppublish
Résumé
The type II secretion system (T2SS) is a multi-protein complex used by many bacteria to move substrates across their cell membrane. Substrates released into the environment serve as local and long-range effectors that promote nutrient acquisition, biofilm formation, and pathogenicity. In both animals and plants, the T2SS is increasingly recognized as a key driver of virulence. The T2SS spans the bacterial cell envelope and extrudes substrates through an outer membrane secretin channel using a pseudopilus. An inner membrane assembly platform and a cytoplasmic motor controls pseudopilus assembly. This microreview focuses on the structure and mechanism of the T2SS. Advances in cryo-electron microscopy are enabling increasingly elaborate sub-complexes to be resolved. However, key questions remain regarding the mechanism of pseudopilus extension and retraction, and how this is coupled with the choreography of the substrate moving through the secretion system. The T2SS is part of an ancient type IV filament superfamily that may have been present within the last universal common ancestor (LUCA). Overall, mechanistic principles that underlie T2SS function have implication for other closely related systems such as the type IV and tight adherence pilus systems.
Substances chimiques
Bacterial Outer Membrane Proteins
0
Bacterial Proteins
0
Type II Secretion Systems
0
Virulence Factors
0
Secretin
1393-25-5
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
412-424Subventions
Organisme : Wellcome Trust
ID : 215553/Z/19/Z
Pays : United Kingdom
Informations de copyright
© 2020 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.
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