دورية أكاديمية

One-helix protein 2 is not required for the synthesis of photosystem II subunit D1 in Chlamydomonas

التفاصيل البيبلوغرافية
العنوان: One-helix protein 2 is not required for the synthesis of photosystem II subunit D1 in Chlamydomonas
المؤلفون: Wang, Fei, Dischinger, Korbinian, Westrich, Lisa Désirée, Meindl, Irene, Egidi, Felix, Trösch, Raphael, Sommer, Frederik, Johnson, Xenie, Schroda, Michael, Nickelsen, Joerg, Willmund, Felix, Vallon, Olivier, Bohne, Alexandra-Viola
المساهمون: Ludwig Maximilian University Munich = Ludwig Maximilians Universität München (LMU), University of Kaiserslautern Kaiserslautern, Biologie du chloroplaste et perception de la lumière chez les micro-algues, Institut de biologie physico-chimique (IBPC (FR_550)), Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Centre National de la Recherche Scientifique (CNRS), Institut de Biosciences et Biotechnologies d'Aix-Marseille (ex-IBEB) (BIAM), Aix Marseille Université (AMU)-Centre National de la Recherche Scientifique (CNRS)-Direction de Recherche Fondamentale (CEA) (DRF (CEA)), Commissariat à l'énergie atomique et aux énergies alternatives (CEA)-Commissariat à l'énergie atomique et aux énergies alternatives (CEA)
المصدر: ISSN: 0032-0889.
بيانات النشر: HAL CCSD
American Society of Plant Biologists
Oxford University Press
سنة النشر: 2023
مصطلحات موضوعية: [SDV.BV.BOT]Life Sciences [q-bio]/Vegetal Biology/Botanics, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology
الوصف: International audience ; In land plants and cyanobacteria, co-translational association of chlorophyll (Chl) to the nascent D1 polypeptide, a reaction center protein of photosystem II (PSII), requires a Chl binding complex consisting of a short-chain dehydrogenase (high chlorophyll fluorescence 244 [HCF244]/uncharacterized protein 39 [Ycf39]) and one-helix proteins (OHP1 and OHP2 in chloroplasts) of the light-harvesting antenna complex superfamily. Here, we show that an ohp2 mutant of the green alga Chlamydomonas (Chlamydomonas reinhardtii) fails to accumulate core PSII subunits, in particular D1 (encoded by the psbA mRNA). Extragenic suppressors arose at high frequency, suggesting the existence of another route for Chl association to PSII. The ohp2 mutant was complemented by the Arabidopsis (Arabidopsis thaliana) ortholog. In contrast to land plants, where psbA translation is prevented in the absence of OHP2, ribosome profiling experiments showed that the Chlamydomonas mutant translates the psbA transcript over its full length. Pulse labeling suggested that D1 is degraded during or immediately after translation. The translation of other PSII subunits was affected by assembly-controlled translational regulation. Proteomics showed that HCF244, a translation factor which associates with and is stabilized by OHP2 in land plants, still partly accumulates in the Chlamydomonas ohp2 mutant, explaining the persistence of psbA translation. Several Chl biosynthesis enzymes overaccumulate in the mutant membranes. Partial inactivation of a D1-degrading protease restored a low level of PSII activity in an ohp2 background, but not photoautotrophy. Taken together, our data suggest that OHP2 is not required for psbA translation in Chlamydomonas, but is necessary for D1 stabilization.
نوع الوثيقة: article in journal/newspaper
اللغة: English
العلاقة: hal-04337791; https://hal.science/hal-04337791Test; https://hal.science/hal-04337791/documentTest; https://hal.science/hal-04337791/file/OHP2_author.pdfTest
DOI: 10.1093/plphys/kiad015
الإتاحة: https://doi.org/10.1093/plphys/kiad015Test
https://hal.science/hal-04337791Test
https://hal.science/hal-04337791/documentTest
https://hal.science/hal-04337791/file/OHP2_author.pdfTest
حقوق: info:eu-repo/semantics/OpenAccess
رقم الانضمام: edsbas.82F7D3C8
قاعدة البيانات: BASE