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Distinct structural modulation of photosystem I and lipid environment stabilizes its tetrameric assembly
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab). Tsinghua University, China.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab). Karolinska Institutet, Sweden.
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Number of Authors: 72020 (English)In: Nature Plants, ISSN 2055-026X, Vol. 6, no 3, p. 314-+Article in journal (Refereed) Published
Abstract [en]

Photosystem I (PSI) is able to form different oligomeric states across various species. To reveal the structural basis for PSI dimerization and tetramerization, we structurally investigated PSI from the cyanobacterium Anabaena. This revealed a disrupted trimerization domain due to lack of the terminal residues of PsaL in the lumen, which resulted in PSI dimers with loose connections between monomers and weaker energy-coupled chlorophylls than in the trimer. At the dimer surface, specific phospholipids, cofactors and interactions in combination facilitated recruitment of another dimer to form a tetramer. Taken together, the relaxed luminal connections and lipid specificity at the dimer interface account for membrane curvature. PSI tetramer assembly appears to increase the surface area of the thylakoid membrane, which would contribute to PSI crowding. Photosystem I from the cyanobacterium Anabaena has a disrupted trimerization domain resulting in dimers with loose connections between monomers. Phospholipids and cofactors at the dimer surface facilitate further dimerization to form a tetramer.

Place, publisher, year, edition, pages
2020. Vol. 6, no 3, p. 314-+
National Category
Biological Sciences Chemical Sciences
Identifiers
URN: urn:nbn:se:su:diva-181067DOI: 10.1038/s41477-020-0610-xISI: 000519577200022PubMedID: 32170279OAI: oai:DiVA.org:su-181067DiVA, id: diva2:1427771
Available from: 2020-05-01 Created: 2020-05-01 Last updated: 2022-02-26Bibliographically approved
In thesis
1. Cryo-EM Studies of Macromolecular Complexes from Photosynthetic Organisms
Open this publication in new window or tab >>Cryo-EM Studies of Macromolecular Complexes from Photosynthetic Organisms
2020 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Plants, algae, and cyanobacteria convert light energy into chemical energy through the process of photosynthesis, fueling the planet and making life as we know it possible. Photosystem I (PSI) is one of the main photosynthetic complexes, responsible for this process. PSI uses the energy of light to transfer electrons from the soluble electron carrier plastocyanin, on the lumenal site of the thylakoid membrane, to ferrodoxin, on the stromal site of the membrane. Thus, playing a key role in the light dependent reactions. In order to survive many photosynthetic organisms need to be able to adapt to fluctuations in light and have adapted their photosynthetic machinery accordingly. In recent years many advances have been made in electron cryo-microscopy, making it possible to visualize many previously elusive photosynthetic complexes. This has brought a wealth of information on the structural adaptations of PSI.

In plants and algae, PSI is hosted by the chloroplast, a specialized organelle that houses the photosynthetic reactions. In the chloroplast, key components of PSI are synthesized by the chloroplasts own translation machinery: the chloroplast ribosome. Translation in the chloroplast is remarkable as it has to synchronize translation in two different genetic compartments as well as adapt to fluctuations in light. A glimpse of how this machinery has evolved to be able to fulfill all of these duties can be obtained from its three dimensional structure and its chloroplast specific features. However, despite all this structural information providing valuable clues as to the functioning of these systems, there are still many aspects of how they play a role that still remain unknown.

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2020. p. 44
Keywords
cryo-EM, membrane proteins, photosynthesis, translation, chloroplast, ribosome, photosystem I, protein structure
National Category
Biochemistry Molecular Biology
Research subject
Biochemistry
Identifiers
urn:nbn:se:su:diva-183859 (URN)978-91-7911-252-3 (ISBN)978-91-7911-253-0 (ISBN)
Public defence
2020-09-25, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
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Available from: 2020-09-02 Created: 2020-08-11 Last updated: 2025-02-20Bibliographically approved

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Perez-Boerema, AnnemarieZhang, LaixingYang, MaojunAmunts, Alexey

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