Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.
Journal
Nature communications
ISSN: 2041-1723
Titre abrégé: Nat Commun
Pays: England
ID NLM: 101528555
Informations de publication
Date de publication:
06 05 2020
06 05 2020
Historique:
received:
11
09
2019
accepted:
19
03
2020
entrez:
8
5
2020
pubmed:
8
5
2020
medline:
15
8
2020
Statut:
epublish
Résumé
Type IV pili are flexible filaments on the surface of bacteria, consisting of a helical assembly of pilin proteins. They are involved in bacterial motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). Here, we use cryo-electron microscopy and mass spectrometry to show that the bacterium Thermus thermophilus produces two forms of type IV pilus ('wide' and 'narrow'), differing in structure and protein composition. Wide pili are composed of the major pilin PilA4, while narrow pili are composed of a so-far uncharacterized pilin which we name PilA5. Functional experiments indicate that PilA4 is required for natural transformation, while PilA5 is important for twitching motility.
Identifiants
pubmed: 32376942
doi: 10.1038/s41467-020-15650-w
pii: 10.1038/s41467-020-15650-w
pmc: PMC7203116
doi:
Substances chimiques
Fimbriae Proteins
147680-16-8
DNA
9007-49-2
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
2231Subventions
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R000484/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 202904/Z/16/Z
Pays : United Kingdom
Organisme : Biotechnology and Biological Sciences Research Council
ID : BB/R008639/1
Pays : United Kingdom
Organisme : Wellcome Trust
ID : 206181/Z/17/Z
Pays : United Kingdom
Organisme : Medical Research Council
ID : MC_U105184326
Pays : United Kingdom
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