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    Home > Food News > Food Articles > China University of Science and Technology reveals the "drill ring" structure of a yeast acetyl transfer enzyme

    China University of Science and Technology reveals the "drill ring" structure of a yeast acetyl transfer enzyme

    • Last Update: 2021-03-10
    • Source: Internet
    • Author: User
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    Diamond Ring can enhance the relationship between two lovers, with a "drill ring" structure of histone acetyl transferase / transactive protein binding protein complex (the compound) can promote a variety of important processes in the organism, including transcription, DNA damage repair and signal conduction. The research team of Professor Cai Gang of China University of Science and Technology and Professor Jacques Cotter of the Cancer Research Center of Laval University of Canada realized a high-precision description of the structure of acetyl transferase in wine-making yeast, revealed the mechanism of assembly and regulation, and described the interaction interface between components. The results were published in the
    20.
    complex is an important acetyl transferase that regulates the stability of the genome of the ceuterocytes. Due to the complexity of its composition and the variability of its composition, it is difficult for traditional analytical methods to achieve sufficient precision, and it is difficult for the academic community to make a breakthrough in the study of the assembly and regulation mechanism of this compound. Using a cryoelectrometer, Professor Cai Gang's team obtained the complex's fine three-dimensional structure at subnomet resolution and clearly demonstrated its assembly process and adjustment interface.the
    study found that a compound that plays an important role in the assembly of the complex, also known as a "fake kinase", is not kinase active, but can take a similar activation-like kinase configuration in the complex, together with another component, to form a stent for the assembly of the complex, leading to the assembly of proteins. At the same time, the mechanism by which this fake kinase operates suggests that other members of the same family are likely to have a "scaffolding" function independent of kinase activity.
    important finding is that mutations in this fake kinase, which is directly related to cancer, are concentrated in the assembly interface of the complex, which is also a hot spot regulated by multiple modifications. This shows that the assembly of the complex and its fine regulation have important physiological significance, which can help us to better understand the mechanism of cancer-related development and accurately identify the markers.
    the compound was significantly reduced in several multiple cancers. Specific inhibitors can therefore be used to treat cancer cells. In the future, Cai Gang's team will focus on analyzing the high-resolution structure of the whole enzyme complex and its substrate selectivity and catalytic process, thus helping the development of specific inhibitors, which is expected to bring about a major breakthrough in personalized treatment of cancer. (Source: Zhongqing Online: Fan Qiong Wang Lei)
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