How Chaperones Protect Virgin Proteins

How the rod-like pili that enable pathogenic bacteria to adhere to host tissues are built up from their protein (pilin) subunits is one of the great wonders of molecular biology. In a Perspective, [Eisenberg][1] describes new findings about how pili are assembled, revealed by analysis of the crystal structures of pili subunits bound to their molecular chaperones ([ Choudhury et al .][2] and [ Sauer et al .][3]). The chaperone proteins transport the pili subunits to the bacterial surface (preventing them from interacting with other proteins prematurely) and release them there, enabling them to attach to the growing pilus rod. [1]: http://www.sciencemag.org/cgi/content/full/285/5430/1021 [2]: http://www.sciencemag.org/cgi/content/short/285/5430/1061 [3]: http://www.sciencemag.org/cgi/content/short/285/5430/1058