Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor

Boerema AP, Aibara S, Paul B, Tobiasson V, Kimanius D, Forsberg BO, Wallden K, Lindahl E, Amunts A

NPLANTS 4 (4) 212-217 [2018-04-00; online 2018-04-02]

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 chlororibosome. Despite recent structural information, 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.

Cryo-EM [Service]

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DOI 10.1038/s41477-018-0129-6

Crossref 10.1038/s41477-018-0129-6

PDB: 6ERI Structure of the chloroplast ribosome with chl-RRF and hibernation-promoting factor
EMDB: EMD-3941 whole chlororibosome
EMDB: EMD-3942 focused refinement of chl-LSU
EMDB: EMD-3943 focused refinement of chl-SSU