Title

Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation

UMMS Affiliation

RNA Therapeutics Institute; Department of Biochemistry and Molecular Pharmacology

Publication Date

2021-09-13

Document Type

Article

Disciplines

Amino Acids, Peptides, and Proteins | Biochemistry | Nucleic Acids, Nucleotides, and Nucleosides

Abstract

When a ribosome encounters the stop codon of an mRNA, it terminates translation, releases the newly made protein, and is recycled to initiate translation on a new mRNA. Termination is a highly dynamic process in which release factors (RF1 and RF2 in bacteria; eRF1*eRF3*GTP in eukaryotes) coordinate peptide release with large-scale molecular rearrangements of the ribosome. Ribosomes stalled on aberrant mRNAs are rescued and recycled by diverse bacterial, mitochondrial, or cytoplasmic quality control mechanisms. These are catalyzed by rescue factors with peptidyl-tRNA hydrolase activity (bacterial ArfA*RF2 and ArfB, mitochondrial ICT1 and mtRF-R, and cytoplasmic Vms1), that are distinct from each other and from release factors. Nevertheless, recent structural studies demonstrate a remarkable similarity between translation termination and ribosome rescue mechanisms. This review describes how these pathways rely on inherent ribosome dynamics, emphasizing the active role of the ribosome in all translation steps.

Keywords

rescue, ribosome, termination, translation

DOI of Published Version

10.1134/S0006297921090066

Source

Korostelev AA. Diversity and Similarity of Termination and Ribosome Rescue in Bacterial, Mitochondrial, and Cytoplasmic Translation. Biochemistry (Mosc). 2021 Sep;86(9):1107-1121. doi: 10.1134/S0006297921090066. PMID: 34565314; PMCID: PMC8943824. Link to article on publisher's site

Journal/Book/Conference Title

Biochemistry. Biokhimiia

Related Resources

Link to Article in PubMed

PubMed ID

34565314

Link to Full Text

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