Nature journal of Tongji University reveals the mechanism of kinesin action
Researchers from the School of Life Science and Technology of Tongji University and the LEBS laboratory of the French National Research Center published an article entitled "Structure of a kinesin–tubulin complex and implications for kinesin motility", which for the first time accurately clarified kinesin and tubulin The interaction mode and binding site reveal the conformation of kinesin when ATP hydrolysis occurs. The research results were published in the journal Nature Structural & Molecular Biology.
The corresponding author of the article is Professor Wang Chunguang of the Protein Research Institute of Tongji University and Dr. Marcel Knossow of the LEBS laboratory of the French National Research Center. The biochemical properties of the interaction between kinesin and tubulin were completed by Wang Weiyi, a doctoral student of Tongji University, and Jiang Qiyang, an undergraduate .
Kinesin is a large class of motor proteins with microtubules as orbits. It can convert the energy produced by hydrolyzing ATP into mechanical energy and is responsible for the intracellular transport of many substances, so it participates in many important biological activities. The transportation of kinesin on microtubules is highly strict and effective. Every ATP hydrolysis event can make kinesin take a step forward on microtubules. In this process, the binding of ATP and kinesin is a key step, which is enough for the kinesin to produce a power stroke. But the structural mechanism of kinesin working process has never been solved at the atomic resolution level.
In this article, by analyzing the crystal structure of kinesin and tubulin complex in the ATP binding state, the researchers precisely clarified for the first time how kinesin interacts with tubulin and the binding site, revealing The conformation of kinesin when ATP is hydrolyzed.
More importantly, it can be clearly seen from the crystal structure of the complex that the binding of kinesin to ATP and tubulin causes the displacement of two α-helices H6 and H4 in the motor domain, respectively. In addition, the Neck linker fragment of kinesin is bound to the surface of the motor domain to form a docking conformation. This is the key conformational change in the working process of kinesin. This result greatly promoted the understanding of the working mechanism of kinesin, and laid the foundation for further research.
In addition, in this magazine, Tongji University recently cooperated with researchers from the Dana-Farber Cancer Institute to use integrated genomic data analysis methods to mine clinically relevant cancer long non-coding RNAs and found two important prostate cancer lncRNAs. gene.
The researchers re-annotated and re-analyzed the Human Exon Array in the public database to study the expression profile of lncRNA in cancer, and combined with Other types of data to mine the role of cancer in cancer lncRNA and biotags that may be used for cancer diagnosis. They combined various omics data to focus on the analysis of prostate cancer, found two important lncRNA genes (named PCAN-R1 and PCAN-R2, respectively), and experimentally verified that these two lncRNAs are indeed in the prostate Cancer plays a role in regulating the growth of cancer cells.
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