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-Structure paper
Title | Conserved heterodimeric GTPase Rbg1/Tma46 promotes efficient translation in eukaryotic cells. |
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Journal, issue, pages | Cell Rep, Vol. 37, Issue 4, Page 109877, Year 2021 |
Publish date | Oct 26, 2021 |
Authors | Fuxing Zeng / Xin Li / Melissa Pires-Alves / Xin Chen / Christopher W Hawk / Hong Jin / |
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, ...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. |
External links | Cell Rep / PubMed:34706231 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.23 Å |
Structure data | EMDB-24652, PDB-7rr5: |
Chemicals | ChemComp-MG: ChemComp-ASP: ChemComp-ZN: |
Source |
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Keywords | RIBOSOME / Rbg1 / Tma46 |