Serine peptidase Vpr forms enzymatically active fibrils outside Bacillus bacteria revealed by cryo-EM.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
18 Nov 2023
18 Nov 2023
Historique:
received:
17
08
2023
accepted:
08
11
2023
medline:
27
11
2023
pubmed:
19
11
2023
entrez:
18
11
2023
Statut:
epublish
Résumé
Bacteria develop a variety of extracellular fibrous structures crucial for their survival, such as flagella and pili. In this study, we use cryo-EM to identify protein fibrils surrounding lab-cultured Bacillus amyloiquefaciens and discover an unreported fibril species in addition to the flagellar fibrils. These previously unknown fibrils are composed of Vpr, an extracellular serine peptidase. We find that Vpr assembles into fibrils in an enzymatically active form, potentially representing a strategy of enriching Vpr activities around bacterial cells. Vpr fibrils are also observed under other culture conditions and around other Bacillus bacteria, such as Bacillus subtilis, which may suggest a general mechanism across all Bacillus bacterial groups. Taken together, our study reveals fibrils outside the bacterial cell and sheds light on the physiological role of these extracellular fibrils.
Identifiants
pubmed: 37980359
doi: 10.1038/s41467-023-43359-z
pii: 10.1038/s41467-023-43359-z
pmc: PMC10657474
doi:
Substances chimiques
Serine Endopeptidases
EC 3.4.21.-
Serine
452VLY9402
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
7503Subventions
Organisme : National Natural Science Foundation of China (National Science Foundation of China)
ID : 32271276
Informations de copyright
© 2023. The Author(s).
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