Summary for 9F9S
| Entry DOI | 10.2210/pdb9f9s/pdb |
| EMDB information | 50259 |
| Descriptor | Uncharacterized protein YEL057C, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, ... (95 entities in total) |
| Functional Keywords | ribosome, quality control, frame shifting, collision |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
| Total number of polymer chains | 164 |
| Total formula weight | 6403531.58 |
| Authors | Denk, T.,Beckmann, R. (deposition date: 2024-05-08, release date: 2024-12-04, Last modification date: 2024-12-18) |
| Primary citation | Kim, K.Q.,Li, J.J.,Nanjaraj Urs, A.N.,Pacheco, M.E.,Lasehinde, V.,Denk, T.,Tesina, P.,Tomomatsu, S.,Matsuo, Y.,McDonald, E.,Beckmann, R.,Inada, T.,Green, R.,Zaher, H.S. Multiprotein bridging factor 1 is required for robust activation of the integrated stress response on collided ribosomes. Mol.Cell, 84:4594-, 2024 Cited by PubMed Abstract: In yeast, multiprotein bridging factor 1 (Mbf1) has been proposed to function in the integrated stress response (ISR) as a transcriptional coactivator by mediating a direct interaction between general transcription machinery and the process's key effector, Gcn4. However, mounting evidence has demonstrated that Mbf1 (and its human homolog EDF1) is recruited to collided ribosomes, a known activator of the ISR. In this study, we connect these otherwise seemingly disparate functions of Mbf1. Our biochemical and structural analyses reveal that Mbf1 functions as a core ISR factor by interacting with collided ribosomes to mediate Gcn2 activation. We further show that Mbf1 serves no role as a transcriptional coactivator of Gcn4. Instead, Mbf1 is required for optimal stress-induced eukaryotic initiation factor 2α (eIF2α) phosphorylation and downstream de-repression of GCN4 translation. Collectively, our data establish that Mbf1 functions in ISR signaling by acting as a direct sensor of stress-induced ribosome collisions. PubMed: 39566505DOI: 10.1016/j.molcel.2024.10.029 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.9 Å) |
Structure validation
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