Summary for 8IP9
Entry DOI | 10.2210/pdb8ip9/pdb |
EMDB information | 35635 |
Descriptor | 18S ribosomal RNA, 40S ribosomal protein uS9, 40S ribosomal protein uS10, ... (37 entities in total) |
Functional Keywords | ribosome, translation |
Biological source | Triticum aestivum (bread wheat) More |
Total number of polymer chains | 35 |
Total formula weight | 1210386.01 |
Authors | Yokoyama, T.,Tanaka, M.,Saito, H.,Nishimoto, M.,Tsuda, K.,Sotta, N.,Shigematsu, H.,Shirouzu, M.,Iwasaki, S.,Ito, T.,Fujiwara, T. (deposition date: 2023-03-14, release date: 2024-02-21, Last modification date: 2024-05-15) |
Primary citation | Tanaka, M.,Yokoyama, T.,Saito, H.,Nishimoto, M.,Tsuda, K.,Sotta, N.,Shigematsu, H.,Shirouzu, M.,Iwasaki, S.,Ito, T.,Fujiwara, T. Boric acid intercepts 80S ribosome migration from AUG-stop by stabilizing eRF1. Nat.Chem.Biol., 20:605-614, 2024 Cited by PubMed Abstract: In response to environmental changes, cells flexibly and rapidly alter gene expression through translational controls. In plants, the translation of NIP5;1, a boric acid diffusion facilitator, is downregulated in response to an excess amount of boric acid in the environment through upstream open reading frames (uORFs) that consist of only AUG and stop codons. However, the molecular details of how this minimum uORF controls translation of the downstream main ORF in a boric acid-dependent manner have remained unclear. Here, by combining ribosome profiling, translation complex profile sequencing, structural analysis with cryo-electron microscopy and biochemical assays, we show that the 80S ribosome assembled at AUG-stop migrates into the subsequent RNA segment, followed by downstream translation initiation, and that boric acid impedes this process by the stable confinement of eukaryotic release factor 1 on the 80S ribosome on AUG-stop. Our results provide molecular insight into translation regulation by a minimum and environment-responsive uORF. PubMed: 38267667DOI: 10.1038/s41589-023-01513-0 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3 Å) |
Structure validation
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