echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Active Ingredient News > Study of Nervous System > Nature: Reveals the mechanism of action of mitochondrial seism selection and assembly complex

    Nature: Reveals the mechanism of action of mitochondrial seism selection and assembly complex

    • Last Update: 2021-03-10
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    Mitochondrials, as cellular energy plants, are vital to the body: they have more than 1,000 different proteins that are necessary for many central metabolic pathways.
    mitochondrial dysfunction can lead to serious diseases, especially neurological and heart diseases.
    to transport proteins and metabolites, mitochondrials contain a special set of so-called β-barrel membrane proteins, which form transport holes in the outer membrane of the mitochondrial.
    so far, scientists have been unable to explain the patterns that drive the sorting and assembly complexes (sorting and assembly, SAM) that drive these β-barrel membrane protein organisms.
    in a new study, a team led by Professor Toshiya Endo of Kyoto University in Japan, Professor Niels Wiedemann and Professor Nikolaus Pfanner of the University of Freiburg in Germany, and Professor Thomas Becker of the University of Bonn have cracked the structure and function of the SAM complex.
    study was recently published in the journal Nature under the title "Mitochondrial sorting and assembly machinery operates by β-barrels."
    SAM complex usually consists of two β-barrel membrane protein sub-base called Sam50, the outer β of which are covered by two other sub-base Sam35 and Sam37.
    the researchers found that while the SAM complex formed a β-barrel membrane protein, it contained only one Sam50.
    the second β-barrel membrane protein sub-base functions as a flexible placeholder: it temporarily leaves the SAM complex to make room for the formation of the new β-barrel membrane protein.
    this dynamic mechanism shows how the new β-barrel membrane protein matures to full size in the SAM complex and can only be released as a fully folded protein.
    we can identify new principles for membrane protein formation that plays a vital role in our cells," explains Wiedemann, a researcher at the U.S. Department of Science and Technology.
    " Reference: 1. Hironori Takeda et al. Mitochondrial sorting and assembly machinery operates by β-barrel switching. Nature, 2021, doi:10.1038/s41586-020-03113-7.2.the basiss for mitochondria, essential cellular powerhouses This article was originally published from Bio Valley, for more information please download Bio Valley APP (
    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.

    Related Articles

    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.