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A new twist on bacterial motility – two distinct type IV pili revealed by cryoEM

By Alexander Neuhaus, Muniyandi Selvaraj, Ralf Salzer, Julian D. Langer, Kerstin Kruse, Kelly Sanders, Bertram Daum, Beate Averhoff, Vicki A. M. Gold

Posted 31 Jul 2019
bioRxiv DOI: 10.1101/720938 (published DOI: 10.1038/s41467-020-15650-w)

Many bacteria express flexible protein filaments on their surface that enable a variety of important cellular functions. Type IV pili are examples of such filaments and are comprised of a helical assembly of repeating pilin subunits. Type IV pili are involved in motility (twitching), surface adhesion, biofilm formation and DNA uptake (natural transformation). They are therefore powerful structures that enable bacterial proliferation and genetic adaptation, potentially leading to the development of pathogenicity and antibiotic resistance. They are also targets for drug development. By a complement of experimental approaches, we show that the bacterium Thermus thermophilus produces two different forms of type IV pilus. We have determined the structures of both and built atomic models. The structures answer key unresolved questions regarding the molecular architecture of type IV pili and identify a new type of pilin. We also delineate the roles of the two filaments in promoting twitching and natural transformation.

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