7RR5

Structure of ribosomal complex bound with Rbg1/Tma46

This is a non-PDB format compatible entry.

Summary for 7RR5

• Entry DOI: 10.2210/pdb7rr5/pdb
• EMDB information: 24652
• Descriptor: 25S rRNA, 60S ribosomal protein L8-A, 60S ribosomal protein L9-A, ... (90 entities in total)
• Functional Keywords: rbg1, tma46, ribosome
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Total number of polymer chains: 87
• Total formula weight: 3339370.28

Authors

Zeng, F.,Li, X.,Pires-Alves, M.,Chen, X.,Hawk, C.W.,Jin, H. (deposition date: 2021-08-09, release date: 2021-11-10, Last modification date: 2024-11-20)

Primary citation

Zeng, F.,Li, X.,Pires-Alves, M.,Chen, X.,Hawk, C.W.,Jin, H.
Conserved heterodimeric GTPase Rbg1/Tma46 promotes efficient translation in eukaryotic cells.
Cell Rep, 37:109877-109877, 2021

PubMed Abstract: Conserved developmentally regulated guanosine triphosphate (GTP)-binding proteins (Drgs) and their binding partner Drg family regulatory proteins (Dfrps) are important for embryonic development, cellular growth control, differentiation, and proliferation. Here, we report that the yeast Drg1/Dfrp1 ortholog Rbg1/Tma46 facilitates translational initiation, elongation, and termination by suppressing prolonged ribosome pausing. Consistent with the genome-wide observations, deletion of Rbg1 exacerbates the growth defect resulting from translation stalling, and Rbg1 stabilizes mRNAs against no-go decay. Furthermore, we provide a cryoelectron microscopy (cryo-EM) structure of the 80S ribosome bound with Rbg1/Tma46 that reveals the molecular interactions responsible for Rbg1/Tma46 function. The Rbg1 subunit binds to the GTPase association center of the ribosome and the A-tRNA, and the N-terminal zinc finger domain of the Tma46 subunit binds to the 40S, establishing an interaction critical for the ribosomal association. Our results answer the fundamental question of how a paused ribosome resumes translation and show that Drg1/Dfrp1 play a critical role in ensuring orderly translation.

PubMed: 34706231
DOI: 10.1016/j.celrep.2021.109877

Experimental method

ELECTRON MICROSCOPY (3.23 Å)