A single protein can self-assemble to build the scaffold for a biomolecular condensate that makes up a key nucleolar compartment. Inside all living cells, loosely formed assemblies known as biomolecular condensates perform many critical functions. However, it is not well understood how proteins a
MIT biologists discovered that a scaffolding protein called TCOF1 is responsible for the formation of a biomolecular condensate called the fibrillar center, which forms within the cell nucleolus, represented in pink inside the purple nucleus. Credit: iStock
The findings could help to explain a major evolutionary shift, which took place around 300 million years ago, in how the nucleolus is organized. Until that point, the nucleolus, whose role is to help build ribosomes, was divided into two compartments. However, in amniotes , the nucleolus developed a condensate that acts as a third compartment. Biologists do not yet fully understand why this shift happened.
Many cell functions are carried out by membrane-bound organelles, such as lysosomes and mitochondria, but membraneless condensates also perform critical tasks such as gene regulation and stress response. In some cases, these condensates form when needed and then dissolve when they are finished with their task.
In the new study, the researchers found that whenever TCOF1 is expressed in cells, condensates form. These condensates always include proteins usually found within a particular condensate known as the fibrillar center of the nucleolus. The FC is known to be involved in the production of ribosomal, a key component of ribosomes, the cell complex responsible for building all cellular proteins.
“What’s really exciting about this work is that it gives us a molecular handle to control a condensate, introduce it into a species that doesn’t have it, and also get rid of it in a species that does have it. That could really help us unlock the structure-to-function relationship and figure out what is the role of the third compartment,” Jaberi-Lashkari says.
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