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    Home > Biochemistry News > Biotechnology News > Sun Fei/Zhang Chuanmao's group of Peking University has made important progress in the study of the outer ring structure of nuclear pore complexes

    Sun Fei/Zhang Chuanmao's group of Peking University has made important progress in the study of the outer ring structure of nuclear pore complexes

    • Last Update: 2022-01-25
    • Source: Internet
    • Author: User
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      On January 11, 2022, " Protein & Cell " published online the latest achievements of Sun Fei's group from the State Key Laboratory of Biomacromolecules and Zhang Chuanmao's group from Peking University in the study of the outer ring structure of the nuclear pore complex of Xenopus laevis"8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI"
    .
    In this study, the cryo-electron microscopy density map of the nuclear pore complex peripheral ring with a resolution of 8 angstroms and near-isotropy was obtained, and on this basis, a complete structural model of the Y complex was constructed, in the asymmetric unit of the cytoplasmic ring 5 Nup358, 2 Nup214 complexes, 2 Nup205 and 1 Nup93 were found in The spatial position and interaction relationship enable the complete analysis of the structural model of the peripheral ring of the nuclear pore complex, laying a foundation for comprehensively revealing the structure and function of the nuclear pore complex

    .

      The nucleus is the largest organelle in eukaryotic cells, and on the nuclear membrane there are pores that communicate the transport of nucleoplasmic and cytoplasmic substances and energy, called the nuclear pore complex
    .
    From the cytoplasmic side to the nucleoplasmic side, the nuclear pore complex can be divided into cytoplasmic fibers, cytoplasmic rings, inner rings, intraluminal rings, nucleoplasmic rings and nuclear baskets

    .
    The nuclear pore complex as a whole presents a quasi-eight-fold symmetrical hollow cylindrical structure surrounding the central channel of the nuclear pore.
    In higher eukaryotes (such as humans, Xenopus, etc.
    ) , the molecular weight can reach more than 100 megadaltons

    .
    Resolving the high-resolution structure of the nuclear pore complex is of great significance for understanding its assembly mechanism and the origin of eukaryotes

    .
    However, due to its huge molecular mass and highly dynamic adaptation to physiological functions, the nuclear pore complex still lacks a reliable high-resolution atomic structure model, which limits the in-depth study of its structure and physiological function

    .
    In 2020, Shi Yigong's team from West Lake University used cryo-electron microscopy single particle analysis and tomography to study the structural characteristics of the cytoplasmic and intraluminal rings of the nuclear pore complex of Xenopus laevis, which can be found in most cytoplasmic ring assemblies.
    Identify and locate secondary structure elements

    .
    In early January this year, Michael Rout's research team in the United States published a paper in the journal
    Cell , using comprehensive techniques to study the high-resolution structure of the yeast nuclear pore complex in the isolated and purified state and the relatively low-resolution structure in the in situ physiological state , elucidating the modularly assembled form of the yeast nuclear pore complex and its relationship to physiological functional states
    .
    These studies have deepened the understanding of the mechanism of NPC assembly

    .

      Sun Fei's research group and Zhang Chuanmao's research group of Peking University have further developed cryo-electron microscopy single particle analysis technology according to the sample characteristics of nuclear pore complexes.
    Nucleopore complexes containing various orientations were obtained for three-dimensional reconstruction calculations

    .
    The final data processing results show that this data collection and processing method can achieve higher resolution than previous reconstruction results using electron tomography, and most of the protein subunits can reach the level of secondary structure resolution.

    .
    An overall resolution of around 8 Angstroms can be achieved for different regions of the outer rings of the nuclear pore complex (i.
    e.
    , the cytoplasmic and nucleoplasmic rings)

    .

    Fig.
    1 The fine structure study of the outer loop of the Xenopus nuclear pore complex reveals the composition and interaction patterns of numerous protein subunits

    .

      On this basis, with the help of AlphaFold2, the most accurate protein three-dimensional structure prediction software, the researchers predicted the full-length three-dimensional structures of all nucleoporins in the Xenopus nuclear pore complex, and based on the high-quality three-dimensional reconstruction results, for The density map of the outer ring of the nuclear pore complex was modeled and modified, and the most complete NPC outer ring structure model was obtained
    .
    This structure not only complements the missing part of the skeleton of the outer ring of the nuclear pore complex, the Y complex (Figure 1), but also identifies a series of nucleoporin subunits that play important functions on the outer ring, clarifying these unknown The fine structure and assembled form of the components

    .
    On each asymmetric unit on the cytoplasmic loop, a Nup358 five-membered protein complex was identified, and two Nup214 complexes were found to form the nuclear export platform of the messenger ribonucleoprotein, and a Nup93 protein played a bridging role to connect the cytoplasm The stem regions of the two Y complexes of the loop and the two Nup205 proteins function to stabilize the cytoplasmic loop structure, respectively

    .
    On each asymmetric unit of the nucleocytoplasmic loop, a Nup205 protein was identified to stabilize the nucleocytoplasmic loop structure, an ELYS protein to initiate anaphase nuclear pore complex assembly, and a Nup93 to bridge the nucleocytoplasmic loop Function of the stem region of the Y complex

    .
    These structural information can provide important reference data for future studies on the assembly of nuclear pore complexes

    .

      Researcher Sun Fei from the Institute of Biophysics, Chinese Academy of Sciences and Prof.
    Zhang Chuanmao from Peking University are the co-corresponding authors of this paper.
    Doctoral student Tai Linhua, researcher Zhu Yun, and postdoctoral fellow are the co-first authors of this paper

    .
    The research was funded by the pilot project of the Chinese Academy of Sciences, the National Natural Science Foundation of China and the key research and development projects of the Ministry of Science and Technology

    .
    The screening of samples for this study was completed in the Electron Microscopy Center, School of Life Sciences, Peking University, and the data collection was completed in the Bioimaging Center of the Institute of Biophysics.
    Special thanks to Dr.
    Xiaojun Huang of the Institute of Biophysics for his support and help in data collection

    .
    The research group of Zhang Lihua, Dalian Institute of Chemical Physics, Chinese Academy of Sciences, and the research group of Professor Fan Jun, City University of Hong Kong also provided help for this research

    .

      Article link: https://link.
    springer.
    com/article/10.
    1007/s13238-021-00895-y

     

    (Contributed by: Fei Fei Research Group)

     

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