Structural characterization and functional insights into the Type II Secretion System of the poly-extremophile Deinococcus radiodurans.
Deinococcus radiodurans
T2SS
cell envelope
cryo-electron microscopy
lipoproteins
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
08 Dec 2023
08 Dec 2023
Historique:
received:
05
10
2023
revised:
07
11
2023
accepted:
28
11
2023
medline:
11
12
2023
pubmed:
11
12
2023
entrez:
10
12
2023
Statut:
aheadofprint
Résumé
The extremophile bacterium D. radiodurans boasts a distinctive cell envelope characterized by the regular arrangement of three protein complexes. Among these, the Type II Secretion System (T2SS) stands out as a pivotal structural component. We used cryo-electron microscopy to reveal unique features, such as an unconventional protein belt (DR_1364) around the main secretin (GspD), and a cap (DR_0940) found to be a separated subunit rather than integrated with GspD. Furthermore, a novel region at the N-terminus of the GspD constitutes an additional second gate, supplementing the one typically found in the outer membrane region. This T2SS was found to contribute to envelope integrity, while also playing a role in nucleic acid and nutrient trafficking. Studies on intact cell envelopes show a consistent T2SS structure repetition, highlighting its significance within the cellular framework.
Identifiants
pubmed: 38072042
pii: S0021-9258(23)02565-6
doi: 10.1016/j.jbc.2023.105537
pii:
doi:
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
105537Informations de copyright
Copyright © 2023 The Authors. Published by Elsevier Inc. All rights reserved.
Déclaration de conflit d'intérêts
Competing interests Authors declare that they have no competing interests.