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    Home > Biochemistry News > Biotechnology News > DeSUMO-enzyme SENP6 regulates the positioning of the silk grain-specific histone CENP-A.

    DeSUMO-enzyme SENP6 regulates the positioning of the silk grain-specific histone CENP-A.

    • Last Update: 2020-08-06
    • Source: Internet
    • Author: User
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    A research paper by Zhu Bing of the Institute of Biophysics of the Chinese Academy of Sciences entitled SENP6-Mediated M18BP1 deSUMOylation regulates regulates cenP-A centromeric published online january 10, 2019 in cell research.
    the study found that deSUMO-enzyme SENP6 regulates the positioning of the silk grain-specific histone CENP-A.
    SENP6 ensures the correct positioning of CENP-A in the filament region by protecting its substrate MIS18 complex, the sub-base M18BP1, from degradation by the umO-dependent ubiquitization pathway.
    silk grain is an important structure on chromosome, in the process of cell division, the microparticle strain on the particle sin forms the kinetic structure, for the spindle microtube to provide attachment site, so that the staining monomer is traction separation, thus ensuring the stable inheritance of genetic information.
    in most eyre, the establishment of silk grains is determined by the apparent regulatory factor of the silk grain-specific histone CENP-A.
    therefore, the regulatory mechanism of THE positioning of the Swire of CENP-A has important biological significance.
    Although some research has been made on the positioning of CENP-A, the new factor of regulating CENP-A may still exist.
    the study found THAT SENP6 regulates CENP-A positioning through genome-wide RNAi high-throughput screening techniques.
    SENP6 affects not only the maintenance of THE IGNP-A, which already has the sly grain positioning, but also the placement of the new CENP-A in the G1 phase.
    THE regulation of CENP-A positioning by SENP6 depends on the ubiquitin degradation pathway of the protein mediated by RNF4. further research
    found that M18BP1 degrades after SENP6 is knocked down.
    in addition, the study also found that the M18BP1 protein SUMO-3 connective PIAS4. Zhu Bing, a researcher at the Institute of
    Biophysics, is the author of the paper, and Fu Hang, a doctoral student of Zhu Bing's research group, and Liu Nan, a Doctor al-Sisi, are the co-first authors of the paper.
    , Dr. Qi Xiangbing and Ma Chunxiao, Ph.D. of the Beijing Institute of Life Sciences, participated in the collaborative research.
    the project was supported by the Ministry of Science and Technology, the National Natural Science Foundation of China and the Chinese Academy of Sciences.
    Source: Institute of Biophysics.
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