Cryo-electron microscopy reveals important protein atomic structures

Release date: 2017-11-02

According to a report by the Physicist Organization Network on the 30th, British scientists used the 2017 Nobel Prize in Chemistry, a cryo-electron microscopy technique, to overcome the structural problems of an important protein involved in gene expression. According to a related paper published in the latest issue of Science, the protein structure shows that the influenza virus can bind to specific sites in the protein, destroying the gene expression ability of the cell, and opening up a study for in-depth study of diseases such as influenza and cancer. door.

This important protein, called cleavage and polyadenylation specific factor (CPF), is a complex enzyme composed of multiple subunits. Gene expression is the process of converting DNA-encoded instructions into proteins. It is involved in many important steps, including enzymatic replication of genes and generation of messenger RNA. Messenger RNA moves from the nucleus to the cytoplasm. Organelles in the cytoplasm assemble proteins according to the instructions of messenger RNA. . The CPF enzyme is an essential player in gene expression, which forms long-chain adenosine molecules, adding a "polyadenosine tail" to the end of each messenger RNA. The length of this tail is closely related to how the messenger RNA is transported out of the nucleus, when it appears in the cell, and how often it is transcribed into protein.

For decades, understanding the structure and function of CPF in healthy cells, and how to fold and assemble it, has become a central problem in the field of gene expression. Scientists have nothing to do with this basic protein. Until the advent of cryo-electron microscopy, this revolutionary tool gave scientists the “super power” to unravel the mystery of the natural structure of large composite proteins.

Larry Passmore, a scientist at the Molecular Biology Laboratory of the British Medical Research Council, led his colleagues to successfully establish an atomic structure model of CPF protein using cryo-electron microscopy technology, and unveiled three sub-structural units of this important protein for the first time. . They also identified a specific site on the CPF protein, and the viral protein preferentially occupied this site, preventing the CPF protein from binding to the messenger RNA, thereby blocking the gene expression process in the cell.

Pasmore said that the atomic structure model of CPF protein, in addition to helping them study the mechanism of action of this important protein in healthy cells, opened a new door for disease research, cancer and other diseases, by studying this " The polyadenylation tail can find new causes and therapies.

Editor-in-chief

The scientific circle has a popular view that technology development is not as high-grade as scientific research. In fact, science and technology are not so well defined, and good science or technology is all about innovation. When the cryo-electron microscopy technology appeared, many of the mysterious microscopic truths would be revealed to the world. No wonder it won the Nobel Prize without any dispute. A small step for the inventor, a big step for humans. I hope that there will be more magical inventions for scientists to pave the way.

Source: Technology Daily

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