Cryo-electron microscopy reveals two distinct type IV pili assembled by the same bacterium.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 32376942.
- Also identified by DOI 10.1038/s41467-020-15650-w and PMC identifier 7203116.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
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.
Medical subject headings
- Fimbriae, Bacterial
- Thermus thermophilus