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Structure of a minimal photosystem I from the green alga Dunaliella salina
Stockholms universitet, Naturvetenskapliga fakulteten, Institutionen för biokemi och biofysik. Stockholms universitet, Science for Life Laboratory (SciLifeLab). Karolinska Institutet, Sweden.
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Antal upphovsmän: 62020 (Engelska)Ingår i: Nature plants, ISSN 2055-026X, Vol. 6, nr 3, s. 321-327Artikel i tidskrift (Refereegranskat) Published
Abstract [en]

Solar energy harnessed by oxygenic photosynthesis supports most of the life forms on Earth. In eukaryotes, photosynthesis occurs in chloroplasts and is achieved by membrane-embedded macromolecular complexes that contain core and peripheral antennae with multiple pigments. The structure of photosystem I (PSI) comprises the core and light-harvesting (LHCI) complexes, which together form PSI-LHCI. Here we determined the structure of PSI-LHCI from the salt-tolerant green alga Dunaliella salina using X-ray crystallography and electron cryo-microscopy. Our results reveal a previously undescribed configuration of the PSI core. It is composed of only 7 subunits, compared with 14-16 subunits in plants and the alga Chlamydomonas reinhardtii, and forms the smallest known PSI. The LHCI is poorly conserved at the sequence level and binds to pigments that form new energy pathways, and the interactions between the individual Lhca1-4 proteins are weakened. Overall, the data indicate the PSI of D. salina represents a different type of the molecular organization that provides important information for reconstructing the plasticity and evolution of PSI. The photosystem I light-harvesting complex from the salt-tolerant green alga Dunaliella salina has a core configuration composed of only seven subunits. This unusual molecular organization could inform the reconstruction of photosystem evolution.

Ort, förlag, år, upplaga, sidor
2020. Vol. 6, nr 3, s. 321-327
Nationell ämneskategori
Biologiska vetenskaper
Identifikatorer
URN: urn:nbn:se:su:diva-180615DOI: 10.1038/s41477-020-0611-9ISI: 000517741300001PubMedID: 32123351OAI: oai:DiVA.org:su-180615DiVA, id: diva2:1424974
Tillgänglig från: 2020-04-20 Skapad: 2020-04-20 Senast uppdaterad: 2022-02-26Bibliografiskt granskad
Ingår i avhandling
1. Cryo-EM Studies of Macromolecular Complexes from Photosynthetic Organisms
Öppna denna publikation i ny flik eller fönster >>Cryo-EM Studies of Macromolecular Complexes from Photosynthetic Organisms
2020 (Engelska)Doktorsavhandling, sammanläggning (Övrigt vetenskapligt)
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.

Ort, förlag, år, upplaga, sidor
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2020. s. 44
Nyckelord
cryo-EM, membrane proteins, photosynthesis, translation, chloroplast, ribosome, photosystem I, protein structure
Nationell ämneskategori
Biokemi Molekylärbiologi
Forskningsämne
biokemi
Identifikatorer
urn:nbn:se:su:diva-183859 (URN)978-91-7911-252-3 (ISBN)978-91-7911-253-0 (ISBN)
Disputation
2020-09-25, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (Engelska)
Opponent
Handledare
Tillgänglig från: 2020-09-02 Skapad: 2020-08-11 Senast uppdaterad: 2025-02-20Bibliografiskt granskad

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Perez-Boerema, AnnemarieCaspy, IdoAmunts, Alexey

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Perez-Boerema, AnnemarieCaspy, IdoAmunts, Alexey
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