6TNU

Yeast 80S ribosome in complex with eIF5A and decoding A-site and P-site tRNAs.

This is a non-PDB format compatible entry.

Summary for 6TNU

• Entry DOI: 10.2210/pdb6tnu/pdb
• EMDB information: 10537
• Descriptor: 18S rRNA, 40S ribosomal protein S6-A, 40S ribosomal protein S7-A, ... (86 entities in total)
• Functional Keywords: eif5a, translation control, translation
• Biological source: Saccharomyces cerevisiae; More
• Total number of polymer chains: 83
• Total formula weight: 3038614.64

Authors

Buschauer, R.,Cheng, J.,Berninghausen, O.,Tesina, P.,Becker, T.,Beckmann, R. (deposition date: 2019-12-10, release date: 2020-04-22, Last modification date: 2024-11-06)

Primary citation

Buschauer, R.,Matsuo, Y.,Sugiyama, T.,Chen, Y.H.,Alhusaini, N.,Sweet, T.,Ikeuchi, K.,Cheng, J.,Matsuki, Y.,Nobuta, R.,Gilmozzi, A.,Berninghausen, O.,Tesina, P.,Becker, T.,Coller, J.,Inada, T.,Beckmann, R.
The Ccr4-Not complex monitors the translating ribosome for codon optimality.
Science, 368:-, 2020

PubMed Abstract: Control of messenger RNA (mRNA) decay rate is intimately connected to translation elongation, but the spatial coordination of these events is poorly understood. The Ccr4-Not complex initiates mRNA decay through deadenylation and activation of decapping. We used a combination of cryo-electron microscopy, ribosome profiling, and mRNA stability assays to examine the recruitment of Ccr4-Not to the ribosome via specific interaction of the Not5 subunit with the ribosomal E-site in This interaction occurred when the ribosome lacked accommodated A-site transfer RNA, indicative of low codon optimality. Loss of the interaction resulted in the inability of the mRNA degradation machinery to sense codon optimality. Our findings elucidate a physical link between the Ccr4-Not complex and the ribosome and provide mechanistic insight into the coupling of decoding efficiency with mRNA stability.

PubMed: 32299921
DOI: 10.1126/science.aay6912

Experimental method

ELECTRON MICROSCOPY (3.1 Å)