echemi logo
Product
  • Product
  • Supplier
  • Inquiry
    Home > Biochemistry News > Microbiology News > Fu Aigen's team at Northwestern University revealed the molecular mechanism of Chlamydomonas reinin's resistance to bright light

    Fu Aigen's team at Northwestern University revealed the molecular mechanism of Chlamydomonas reinin's resistance to bright light

    • Last Update: 2023-01-01
    • Source: Internet
    • Author: User
    Search more information of high quality chemicals, good prices and reliable suppliers, visit www.echemi.com
    Please click "PlantReports" above ↑ Follow us! Be the first to know the latest research progress in the field of plant science! The development and utilization of biomass energy with photosynthetic microalgae as the chassis is one of the important ways and measures for the global response to climate change and energy security in the
    future.
    The results show that under strong light irradiation, the photosystem II of photosynthetic organisms is damaged, the photosynthetic efficiency is inhibited, and photosuppression becomes one of the limiting factors of
    light energy conversion and utilization.
    Therefore, it is of great significance
    to deeply analyze the repair mechanism of microalgae photosynthetic system under strong light and explore the key regulatory factors for the improvement of biomass yield.



    Recently, Professor Fu Aigen of Northwest University published a report entitled "Immunophilin CYN28 is required for accumulation of photosystem II and thylakoid FtsH protease in Chlamydomonas" online in Plant Physiology The paper is the first to report a molecular mechanism
    by which the pro-immune protein CYN28, localized in the thylakoid lumen, is involved in Chlamydomonas against high light.



    Pro-proteins are evolutionarily very conserved protein families
    .
    There are a large number of chloroplast thyroidoid lumen in higher plants and Chlamydomonas reininthine, with unknown function.

    This study found that Chlamydomonas reintifoli CYN28 knockout mutant had a typical highlight-sensitive phenotype, with reduced photosystem II accumulation and impaired
    photosystem II repair under bright light.
    In vivo and in vitro biochemical experiments showed that CYN28 had peptidyl prolyl cis- and trans-isomerase (PPIase) activity, and arginine at the 187th position of the conserved site determined its enzymatic activity, which in turn affected the physiological function
    of CYN28.
    The team further used co-immunoprecipitation and protein profiling to identify thylakoid FtsH protease as a downstream target of CYN28, and proved that FtsH N'telproline is the site of action of CYN28
    .
    Deletion of CYN28 or mutation of FtsH N' teloproline can impair
    FtsH protease turnover under bright light.
    Thylakoid membrane FtsH is one of
    the AAA family proteases involved in photosystem II damage repair.
    Previous studies have shown that mutants of Chlamydomonas reinhardi with reduced FtsH expression in photosynthetic organisms also have similar high-light-sensitive phenotypes, while overexpression of FtsH can enhance the ability of Chlamydomonas to resist bright light (Wang et al.
    , 2017; Malnoë et al.
    , 2014)



    In summary, this study reveals that the prophilic protein CYN28 is involved in the high-light resistance
    of Chlamydomonas reinfield by affecting the accumulation of photosystem II and assisting the repair of photosystem II by participating in the turnover under FtsH high light.


    Weihan Fu, a 2019 master's student in the School of Life Sciences of Northwest University, is the first author of the paper, and Professor Fu Aigen and Associate Professor Faye Wong of the School of Life Sciences, Northwest University are the co-corresponding authors
    of the paper.
    The research was supported
    by the National Natural Science Gene, the Science and Technology Department of Shaanxi Province, and the university-level scientific research start-up fund of Northwest University.


    References: Malnoë A, Wang F, Girard-Bascou J, Wollman FA, de Vitry C.
    2014.
    Thylakoid FtsH protease contributes to photosystem II and cytochrome b6f remodeling in Chlamydomonas reinhardtii under stress conditions.
    The Plant Cell.
    26: 373-390.
    Wang F, Qi Y, Malnoë A, Choquet Y, Wollman FA, de Vitry C.
    2017.
    The high light response of thylakoid FtsH protease in Chlamydomonas reinhardtii.
    Molecular Plant.
    10: 99-114.

    This article is transferred from the Plant Physiol public account, only for sharing and communication, without any commercial use
    .
    Click "Read Original" in the lower left corner to view the full text of
    the paper.


    Long press the QR code below to follow Plant Reports!

    Follow the latest research progress in agricultural science and plant science!

    Please contact plantreports@163.
    com for casting and reprinting

    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.