RT Journal Article
SR Electronic
T1 A new twist on bacterial motility – two distinct type IV pili revealed by cryoEM
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 720938
DO 10.1101/720938
A1 Alexander Neuhaus
A1 Muniyandi Selvaraj
A1 Ralf Salzer
A1 Julian D. Langer
A1 Kerstin Kruse
A1 Kelly Sanders
A1 Bertram Daum
A1 Beate Averhoff
A1 Vicki A. M. Gold
YR 2019
UL http://biorxiv.org/content/early/2019/08/12/720938.abstract
AB 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.