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Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics. Stockholm University, Science for Life Laboratory (SciLifeLab).
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2018 (English)In: Nature Plants, ISSN 2055-026X, Vol. 4, p. 212-217Article in journal (Refereed) Published
Abstract [en]

Oxygenic photosynthesis produces oxygen and builds a variety of organic compounds, changing the chemistry of the air, the sea and fuelling the food chain on our planet. The photochemical reactions underpinning this process in plants take place in the chloroplast. Chloroplasts evolved ~1.2 billion years ago from an engulfed primordial diazotrophic cyanobacterium, and chlororibosomes are responsible for synthesis of the core proteins driving photochemical reactions. Chlororibosomal activity is spatiotemporally coupled to the synthesis and incorporation of functionally essential co-factors, implying the presence of chloroplast-specific regulatory mechanisms and structural adaptation of the chlororibosome1,2. Despite recent structural information3,4,5,6, some of these aspects remained elusive. To provide new insights into the structural specialities and evolution, we report a comprehensive analysis of the 2.9–3.1 Å resolution electron cryo-microscopy structure of the spinach chlororibosome in complex with its recycling factor and hibernation-promoting factor. The model reveals a prominent channel extending from the exit tunnel to the chlororibosome exterior, structural re-arrangements that lead to increased surface area for translocon binding, and experimental evidence for parallel and convergent evolution of chloro- and mitoribosomes.

Place, publisher, year, edition, pages
2018. Vol. 4, p. 212-217
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Biological Sciences Chemical Sciences
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URN: urn:nbn:se:su:diva-156633DOI: 10.1038/s41477-018-0129-6ISI: 000430648300011OAI: oai:DiVA.org:su-156633DiVA, id: diva2:1210400
Available from: 2018-05-28 Created: 2018-05-28 Last updated: 2018-05-28Bibliographically approved

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Perez Boerema, AnnemarieAibara, ShintaroTobiasson, VictorKimanius, DariForsberg, Björn O.Walldén, KarinLindahl, ErikAmunts, Alexey
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Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
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