In a study in Nature last week (March 15), researchers report that they have created a 3-D model of the nuclear pore complex in Saccharomyces cerevisiae yeast cells. The architecture of the gateway, which spans the nuclear envelope and allows molecules to enter and leave a cell’s nucleus, shares engineering principles found in large-scale construction projects.
“It reminds us of a suspension bridge, in which a combination of sturdy and flexible parts produce a stress-resilient structure,” says coauthor Michael Rout, a biochemist at the Rockefeller University, in a statement. Rout began mapping the complex more than 20 years ago with his colleague Brian Chait, a biochemist at Rockefeller.
The nuclear pore complex comprises 552 proteins, called nucleoporins, and the model assembled by Rout and colleagues is the first comprehensive map showing how they all fit together. The gateway has diagonal columns and connector cables that make it strong and flexible. The researchers hope their map will enable further study of how the portal functions and how abnormalities in it contribute to disease.
S.J. Kim et al., “Integrative structure and functional anatomy of a nuclear pore complex,” Nature, doi:10.1038/nature26003, 2018.