Nuclear export of pre-60S particles through the nuclear pore complex
© CHRISTOPH BURGSTEDT/SCIENCE PHOTO LIBRARY/Getty Images
A structural study has revealed important clues about how a cell protein factory is itself constructed.
Ribosomes are macromolecular factories that produce proteins according to instructions given by messenger RNA. They consist of two subunits: a smaller one (40S) that decodes messenger RNA and a larger one (60S) that assembles protein pieces.
60S itself is constructed in process that begins in the cell nucleus and ends outside it. But many aspects of this process remain unclear.
Now, a team led by researchers from SUSTech in Shenzhen, China, has used cryo-electron microscopy to determine the structure of particles that are put together to form 60S in yeast.
The pre-60S particles were trapped in the nuclear pore complex — a gateway between the nucleus and the rest of the cell. The structural analysis revealed previously unknown factors that assist with the export of the pre-60s particle from the nucleus.
- Nature 618, 411–418 (2023). doi: 10.1038/s41586-023-06128-y
|Southern University of Science and Technology (SUSTech), China||0.57|
|Beijing Advanced Innovation Center for Structural Biology (ICSB-BJ), China||0.31|
|Peking University (PKU), China||0.11|