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- Title
A conserved set of pilin-like molecules controls type IV pilus dynamics and organelle-associated functions inNeisseria gonorrhoeae.
- Authors
Winther-Larsen, Hanne C.; Wolfgang, Matthew; Dunham, Steven; van Putten, Jos P. M.; Dorward, David; Løvold, Cecilia; Aas, Finn Erik; Koomey, Michael
- Abstract
Type IV pili (Tfp) play central roles in prokaryotic cell biology and disease pathogenesis. As dynamic filamentous polymers, they undergo rounds of extension and retraction modelled as pilin subunit polymerization and depolymerization events. Currently, the molecular mechanisms and components influencing Tfp dynamics remain poorly understood. UsingNeisseria gonorrhoeaeas a model system, we show that mutants lacking any one of a set of five proteins sharing structural similarity to the pilus subunit are dramatically reduced in Tfp expression and that these defects are suppressed in the absence of the PilT pilus retraction protein. Thus, these molecules are not canonical assembly factors but rather act as effectors of pilus homeostasis by promoting extension/polymerization events in the presence of PilT. Furthermore, localization studies support the conclusion that these molecules form a Tfp-associated complex and influence levels of PilC, the epithelial cell adhesin, in Tfp-enriched shear fractions. This is the first time that the step at which individual pilin-like proteins impact on Tfp expression has been defined. The findings have important implications for understanding Tfp dynamics and fundamental Tfp structure/function relationships.
- Subjects
NEISSERIA gonorrhoeae; PROTEINS; POLYMERIZATION; HOMEOSTASIS; EPITHELIAL cells; BIOMOLECULES; CYTOLOGY; MOLECULAR microbiology
- Publication
Molecular Microbiology, 2005, Vol 56, Issue 4, p903
- ISSN
0950-382X
- Publication type
Article
- DOI
10.1111/j.1365-2958.2005.04591.x