دورية أكاديمية
أعرض في EDS

Hydrophobic Mismatch in the Thylakoid Membrane Regulates Photosynthetic Light Harvesting.

التفاصيل البيبلوغرافية
العنوان: Hydrophobic Mismatch in the Thylakoid Membrane Regulates Photosynthetic Light Harvesting.
المؤلفون: Wilson S; Department of Biochemistry, School of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, United Kingdom., Clarke CD; Department of Biochemistry, School of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, United Kingdom., Carbajal MA; Centre for Ultrastructural Imaging, King's College London, London SE1 1UL, United Kingdom., Buccafusca R; Department of Chemistry, School of Physical and Chemical Sciences, Queen Mary University of London, London E1 4NS, United Kingdom., Fleck RA; Centre for Ultrastructural Imaging, King's College London, London SE1 1UL, United Kingdom., Daskalakis V; Department of Chemical Engineering, School of Engineering, University of Patras, Patras 26504, Greece., Ruban AV; Department of Biochemistry, School of Biological and Behavioural Sciences, Queen Mary University of London, London E1 4NS, United Kingdom.
المصدر: Journal of the American Chemical Society [J Am Chem Soc] 2024 May 29; Vol. 146 (21), pp. 14905-14914. Date of Electronic Publication: 2024 May 17.
نوع المنشور: Journal Article
اللغة: English
بيانات الدورية: Publisher: American Chemical Society Country of Publication: United States NLM ID: 7503056 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 1520-5126 (Electronic) Linking ISSN: 00027863 NLM ISO Abbreviation: J Am Chem Soc Subsets: MEDLINE
أسماء مطبوعة: Publication: Washington, DC : American Chemical Society
Original Publication: Easton, Pa. [etc.]
مواضيع طبية MeSH: Thylakoids*/metabolism , Thylakoids*/chemistry , Hydrophobic and Hydrophilic Interactions* , Light-Harvesting Protein Complexes*/metabolism , Light-Harvesting Protein Complexes*/chemistry , Photosynthesis* , Photosystem II Protein Complex*/metabolism , Photosystem II Protein Complex*/chemistry, Galactolipids/metabolism ; Galactolipids/chemistry ; Light
مستخلص: The ability to harvest light effectively in a changing environment is necessary to ensure efficient photosynthesis and crop growth. One mechanism, known as qE, protects photosystem II (PSII) and regulates electron transfer through the harmless dissipation of excess absorbed photons as heat. This process involves reversible clustering of the major light-harvesting complexes of PSII (LHCII) in the thylakoid membrane and relies upon the ΔpH gradient and the allosteric modulator protein PsbS. To date, the exact role of PsbS in the qE mechanism has remained elusive. Here, we show that PsbS induces hydrophobic mismatch in the thylakoid membrane through dynamic rearrangement of lipids around LHCII leading to observed membrane thinning. We found that upon illumination, the thylakoid membrane reversibly shrinks from around 4.3 to 3.2 nm, without PsbS, this response is eliminated. Furthermore, we show that the lipid digalactosyldiacylglycerol (DGDG) is repelled from the LHCII-PsbS complex due to an increase in both the p K a of lumenal residues and in the dipole moment of LHCII, which allows for further conformational change and clustering in the membrane. Our results suggest a mechanistic role for PsbS as a facilitator of a hydrophobic mismatch-mediated phase transition between LHCII-PsbS and its environment. This could act as the driving force to sort LHCII into photoprotective nanodomains in the thylakoid membrane. This work shows an example of the key role of the hydrophobic mismatch process in regulating membrane protein function in plants.
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المشرفين على المادة: 0 (Light-Harvesting Protein Complexes)
0 (Photosystem II Protein Complex)
0 (digalactosyldiacylglycerol)
0 (Galactolipids)
تواريخ الأحداث: Date Created: 20240517 Date Completed: 20240529 Latest Revision: 20240603
رمز التحديث: 20240603
مُعرف محوري في PubMed: PMC11140739
DOI: 10.1021/jacs.4c05220
PMID: 38759103
قاعدة البيانات: MEDLINE
الوصف
تدمد:1520-5126
DOI:10.1021/jacs.4c05220