echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Biochemistry News > Biotechnology News > Chromatin remodeling pathogenesis revealed by Snf2-nuclear small complex structure

    Chromatin remodeling pathogenesis revealed by Snf2-nuclear small complex structure

    • Last Update: 2020-09-06
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    On April 19, 2017, Chen Zhucheng of Tsinghua University's School of Life Sciences and Li Xueming's team published an online article in the journal Nature entitled "Snf2- Nuclear Small Complex Structures" in the journal Nature. The research paper on the revealed chromatin remodeling mechanism (Mechanism of chromatin remodeling revealed by the Snf2-nucleosome structure) explains how Snf2 binds to substrate nucleosomes and the mechanism by which chromatin remodeling occurs.
    cells, DNA is wrapped around histones to form the basic components of chromosomes, nucleosomes.
    chromosomes play a key role in packaging and protecting genetic material.
    chromatin formation at the same time on some physiological processes within the cell, such as DNA replication, transcription, repair and so on have a huge obstacle.
    SWI/SNF family chromatin remodeling complex is widely involved in regulating different biological processes such as stem cell differentiation, reprogramming, immune response, learning and memory, and cancer by regulating the structure of chromatin by using the energy of ATP hydrolysing.
    chromatin remodeling complex from yeast to people are conservative, but the molecular structure of its function is not yet known, is a long-standing chromatin biology field of the basic problem.
    2016 paper published in NSMB by Chen Zhucheng's research team analyzed the structure of Snf2 protein-based crystals and explained Snf2's self-inhibition.
    the structure of the protein binding to the substrate nucleosome is still unknown.
    Other international research groups analytical chromatin remodeling complex and nuclear small body binding structural resolution is at the level of 20 , can only be from the outline and space size to speculate on the binding position of nuclear small bodies , can not solve deeper biological problems, such as how proteins and substrate nucleosomes interact, proteins and how to use the energy of ATP hydrolytic changes in the structure of nuclear small bodies and so on are not known.
    this study, using the frozen electron mirror single particle technology, successfully obtained Snf2-nucleosome resolution of 4.69 s of the electroscope structure (Figure a).
    comparing the crystal structure of the Snf2 protein and the electroscopic structure of the complex previously solved in this laboratory, it was found that after the Snf2 protein binds to the nucleosome, a rotation of about 80 degrees occurs between the two main domains (core1 and core2).
    this huge structural change creates a new interface of interactions mediated by SuppH helix and Brace helix, and pulls together the motif VI (arginine fingers) and motiv I (P-loop), revealing the mechanism by which the nucleosome can stimulate the activity of the Snf2 protein ATP enzyme.
    Unlike the previously thought model of Snf2 functioning between DNA and histones, the results show that Snf2 binds mainly through the phosphate skeletons of multiple conservative deconsective enzyme motif and nucleosome DNA, which also explains the non-specificity of the sequence of chromosomal remodeling complexes binding to DNA, and also reveals a common mechanism for chromosomal remodeling proteins to bind to substrates.
    study, the Snf2 protein breaks the local DNA-histoprotein interaction, deforming the DNA at the binding point.
    the study concluded that ATP binding and hydrolysing led to further structural changes in Snf2, pushing the DNA out, consistent with the "DNA wave" model of chromatin remodeling in the literature.
    this study analyzed the high-resolution structure of the first chromatin remodeling protein binding to the substrate nucleosome, revealing for the first time the agent of chromatin remodeling (Figure b).
    Li Xueming and Chen Zhu are co-authors of this paper, and Liu Xiaoyu, Li Meijing and Xia Xian, Ph.D. students in the School of Life Sciences of Tsinghua University, are co-authors of this paper (Figure c).
    freezing electroscope platform of Tsinghua University, a national protein science research facility in Beijing, provides support for data collection, and Tsinghua University's high-performance computing platform supports data processing.
    study was supported by Tsinghua University's High-Level Innovation Center for Structural Biology, the Joint Center for Life Sciences, the Ministry of Science and Technology, the National Natural Science Foundation of China and the Youth 1,000-person Program of the Central Group Department.
    .
    This article is an English version of an article which is originally in the Chinese language on echemi.com and is provided for information purposes only. This website makes no representation or warranty of any kind, either expressed or implied, as to the accuracy, completeness ownership or reliability of the article or any translations thereof. If you have any concerns or complaints relating to the article, please send an email, providing a detailed description of the concern or complaint, to service@echemi.com. A staff member will contact you within 5 working days. Once verified, infringing content will be removed immediately.

    Contact Us

    The source of this page with content of products and services is from Internet, which doesn't represent ECHEMI's opinion. If you have any queries, please write to service@echemi.com. It will be replied within 5 days.

    Moreover, if you find any instances of plagiarism from the page, please send email to service@echemi.com with relevant evidence.