PerspectiveStructural Biology

How Chaperones Protect Virgin Proteins

See allHide authors and affiliations

Science  13 Aug 1999:
Vol. 285, Issue 5430, pp. 1021-1022
DOI: 10.1126/science.285.5430.1021

You are currently viewing the summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution


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 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. and Sauer et al.). 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.