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    Home > Biochemistry News > Biotechnology News > Competition between hMTR4 and ALYREF plays a role in maintaining the balance between intracellular degradation and out-of-nucleation.

    Competition between hMTR4 and ALYREF plays a role in maintaining the balance between intracellular degradation and out-of-nucleation.

    • Last Update: 2020-08-17
    • Source: Internet
    • Author: User
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    The latest research from Cheng Hong Research Group, Institute of Biochemistry and Cell Biology, Shanghai Institute of Life Sciences, Chinese Academy of Sciences, with exosome cofactor hMTR4 compets with export adaptor ALYREF to curd balanced nuclear RNA for degradation and export, published online, reveals that the competition between hMTR4 and ALYREF plays an important role in maintaining the balance between intracellular degradation and nucleology. Every step of
    gene expression is closely monitored, and the exosome complex is an important part of RNA quality monitoring systems.
    it is a multi-sub-sub-body complex with endoenzyme activity and 3'-5 exsothyase activity that can be involved in processing and degrading a variety of RNA.
    hMTR4 as an important auxiliary protein is indispensable in the function of exosome in the nucleus.
    so far, the base of the exosome complex is numerous, and the substrate identification mechanism is a fundamental problem with exosome.
    , the molecular mechanism sway that RNA degradation or nucleation in the nucleus determines the fate of the nucleus is unclear.
    researchers found and confirmed that a significant portion of mRNA and long non-coding RNA are degraded substrates of the exosome complex in cells that are normally functioning in RNA processing and nucleation.
    by studying the recruitment mechanism of the exosome complex, it is revealed that hMTR4 can recruit the exosome complex to its substrate RNA in a unique way.
    interestingly, this recruitment specificity is achieved through the competition of hMTR4 with the mRNA nucleojoint protein ALYREF in combination with CBC (cap-binding complex).
    researchers provide further evidence to support such a competitive mechanism that determines whether RNA in the nucleus is going to develop or degrade, and may ensure a balance of RNA pools that occur or degrade.
    the research was completed in cooperation with Li Guohui, a researcher at the Dalian Institute of Chemical Physics of the Chinese Academy of Sciences, and his research team, which was supported by the Ministry of Science and Technology and the National Natural Science Foundation of China.
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