Researchers from Harvard University, the University of Colorado and others used a transmission electron microscope (TEM) to observe the proteasome complex responsible for protein degradation in the cell and analyzed its high-resolution 3D structure. The research was published in the recent "Nature" magazine. Our body maintains homeostasis by producing and degrading proteins and controlling many cellular processes. The proteasome complex acts as a waste disposal system when it needs to be regulated and is responsible for degrading cellular proteins. Mutations in the proteasome complex can lead to diseases such as cancer, neurodegenerative diseases, and autoimmune diseases.

Currently, an anti-cancer drug called Velcade is used to reduce proteasome function and treat multiple myeloma. For more than 20 years, scientists have been working on proteasome complex research with a view to developing more effective anti-cancer drugs and treatments with fewer side effects. However, since the proteasome complex is composed of about 30 different proteins, its size is large and the structure is complex, there are many difficulties in understanding the function of the proteasome by analyzing its 3D structure. The proteasome is a protein complex that degrades the "matrix conjugated to ubiquitin". "26S proteasome" is composed of a core particle (CP) and a regulatory particle (RP) formed by a "base" and a "lid". Because Bio TEM technology requires fewer samples and can analyze large-scale protein complexes. In this article, the research team replaced the commonly used protein crystallography technique with this technique.

They inserted the protein sample into the Bio TEM, took hundreds of photos from various angles, and then analyzed the structure and function of the composite of the "pedestal-CP" complex using a high-performance computer. The results showed that the core particles had 7 pockets, and the 6 tails of the control particles entered these pockets. When the two particles are combined, they give the proteasome the ability to process unnecessary proteins in the cell. Professor Ho-Min Kim of the Department of Biomedical Science and Engineering of the Korea Institute of Science and Technology (KAIST) said: "Determining the assembly process and 3D structure of the proteasome complex will enhance our understanding of the protein degradation process in cells Help to promote the development of new drugs. Using Bio TEM, researchers can observe and analyze high-resolution protein structures of large protein complexes that are difficult to handle with protein crystallography. If protein crystallography and Bio TEM can be complementary, It will bring great synergy to the analysis of complex 3D structures of proteins in the future. "

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