What is it about?
Type IVa pili (T4aP) are ubiquitous cell surface filaments important for a variety of processes including motility on surfaces, which depends on cycles of T4aP extension, surface adhesion, and retraction. Because T4aP adhere strongly to surfaces, cells are pulled forward during retractions. We solved the structure of the most rigid and strongest T4aP yet described.
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Why is it important?
A T4aP filament is composed of thousands of copies of the major pilin. It is the tight packing of the major pilin and the large major pilin size, which enables the formation of such dense and rigid T4aP structure with distinct mechanical properties. Interestingly, large major T4a pilins are found in several bacterial phyla and might represent an evolutionary adaptation to specific environments.
Perspectives
Our results advance our understanding of how sequence divergence of major T4a pilins shapes the functional properties of T4aP. In future studies, it will be interesting to obtain structures of T4aP formed by large major pilins from different bacteria to further reveal the potential role of these distinct mechanical properties in T4aP-dependent function. Moreover, the information gained from the first complete T4aP model, composed of major pilins, four minor pilins, and a large PilY1 adhesin, might contribute to a better understanding of the distinct roles performed by these five proteins within the tip complex. Great collaboration with Edward E. Egelman and Yves Dufrêne
Anke Treuner-Lange
Max Planck Institute for Terrestrial Microbiology, Marburg, Germany
Read the Original
This page is a summary of: Tight-packing of large pilin subunits provides distinct structural and mechanical properties for the
Myxococcus xanthus
type IVa pilus, Proceedings of the National Academy of Sciences, April 2024, Proceedings of the National Academy of Sciences,
DOI: 10.1073/pnas.2321989121.
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