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The ribosome termination complex remodels release factor RF3 and ejects GDP.
Nat Struct Mol Biol
December 2024
Department of Microbiology and Immunology, University of Texas Medical Branch, Galveston, TX, USA.
Article Synopsis
- Translation termination involves proteins RF1, RF2, and RF3, with RF3 recycling the other two from the ribosome by exchanging GDP for GTP.
- The research uses cryogenic-electron microscopy to illustrate how the 70S ribosome complex accelerates the release of GDP from RF3, highlighting its role as a guanine nucleotide exchange factor.
- The study reveals that the ribosome remodels RF3, facilitating GTP binding and the release of RF1, showcasing a previously unrecognized function of the ribosome in regulating RF3's activity.
Ribosomal collision is not a prerequisite for ZNF598-mediated ribosome ubiquitination and disassembly of ribosomal complexes by ASCC.
Nucleic Acids Res
May 2024
Department of Cell Biology, SUNY Downstate Health Sciences University, Brooklyn, NY, USA.
Ribosomal stalling induces the ribosome-associated quality control (RQC) pathway targeting aberrant polypeptides. RQC is initiated by K63-polyubiquitination of ribosomal protein uS10 located at the mRNA entrance of stalled ribosomes by the E3 ubiquitin ligase ZNF598 (Hel2 in yeast). Ubiquitinated ribosomes are dissociated by the ASC-1 complex (ASCC) (RQC-Trigger (RQT) complex in yeast).
View Article and Find Full Text PDFRACK1 release from the Ribosome Couples Translational Regulation with Starving Signaling and Possibly Depends on Phosphorylation of Key Serine and Threonine Residues.
Cell Mol Biol (Noisy-le-grand)
January 2023
Molecular Histology and Cell Growth Unit, National Institute of Molecular Genetics "Fondazione Romeo e Enrica Invernizzi" - INGM, Milan, Italy.
The balance between protein anabolism and catabolism sets the foundations on which cells build their homeostasis. RACK1 is a ribosome-associated scaffold protein involved in signal transduction. On the ribosome, RACK1 enhances specific translation.
View Article and Find Full Text PDFRibosome-bound Upf1 forms distinct 80S complexes and conducts mRNA surveillance.
RNA
December 2022
Department of Microbiology and Physiological Systems, UMass Chan Medical School, Worcester, Massachusetts 01655, USA.
Upf1, Upf2, and Upf3, the central regulators of nonsense-mediated mRNA decay (NMD), appear to exercise their NMD functions while bound to elongating ribosomes, and evidence for this conclusion is particularly compelling for Upf1. Hence, we used selective profiling of yeast Upf1:ribosome association to define that step in greater detail, understand whether the nature of the mRNA being translated influences Upf1:80S interaction, and elucidate the functions of ribosome-associated Upf1. Our approach has allowed us to clarify the timing and specificity of Upf1 association with translating ribosomes, obtain evidence for a Upf1 mRNA surveillance function that precedes the activation of NMD, identify a unique ribosome state that generates 37-43 nt ribosome footprints whose accumulation is dependent on Upf1's ATPase activity, and demonstrate that a mutated form of Upf1 can interfere with normal translation termination and ribosome release.
View Article and Find Full Text PDFThe human SKI complex regulates channeling of ribosome-bound RNA to the exosome via an intrinsic gatekeeping mechanism.
Mol Cell
February 2022
Department of Structural Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Munich, Germany. Electronic address:
Article Synopsis
- - The superkiller (SKI) complex is important for RNA degradation in human cells and is linked to the congenital disorder trichohepatoenteric syndrome when it malfunctions.
- - Researchers studied the structure of the human SKI complex in different functional states, focusing on its interaction with ribosomes and RNA.
- - The SKI complex has a unique gating system that controls RNA movement, switching from a closed to an open conformation, which is essential for RNA processing and is similar in other helicase-exosome complexes.
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