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Vms1p is a release factor for the ribosome-associated quality control complex

Author

Listed:
  • Olga Zurita Rendón

    (Howard Hughes Medical Institute
    University of Utah School of Medicine)

  • Eric K. Fredrickson

    (University of Utah School of Medicine)

  • Conor J. Howard

    (University of California, San Francisco
    California Institute for Quantitative Biomedical Research)

  • Jonathan Van Vranken

    (University of Utah School of Medicine)

  • Sarah Fogarty

    (Howard Hughes Medical Institute
    University of Utah School of Medicine)

  • Neal D. Tolley

    (University of Utah)

  • Raghav Kalia

    (University of Utah School of Medicine
    University of California, San Francisco
    California Institute for Quantitative Biomedical Research)

  • Beatriz A. Osuna

    (University of California, San Francisco
    University of California, San Francisco)

  • Peter S. Shen

    (University of Utah School of Medicine)

  • Christopher P. Hill

    (University of Utah School of Medicine)

  • Adam Frost

    (University of Utah School of Medicine
    University of California, San Francisco
    California Institute for Quantitative Biomedical Research
    Chan Zuckerberg Biohub)

  • Jared Rutter

    (Howard Hughes Medical Institute
    University of Utah School of Medicine)

Abstract

Eukaryotic cells employ the ribosome-associated quality control complex (RQC) to maintain homeostasis despite defects that cause ribosomes to stall. The RQC comprises the E3 ubiquitin ligase Ltn1p, the ATPase Cdc48p, Rqc1p, and Rqc2p. Upon ribosome stalling and splitting, the RQC assembles on the 60S species containing unreleased peptidyl-tRNA (60S:peptidyl–tRNA). Ltn1p and Rqc1p facilitate ubiquitination of the incomplete nascent chain, marking it for degradation. Rqc2p stabilizes Ltn1p on the 60S and recruits charged tRNAs to the 60S to catalyze elongation of the nascent protein with carboxy-terminal alanine and threonine extensions (CAT tails). By mobilizing the nascent chain, CAT tailing can expose lysine residues that are hidden in the exit tunnel, thereby supporting efficient ubiquitination. If the ubiquitin–proteasome system is overwhelmed or unavailable, CAT-tailed nascent chains can aggregate in the cytosol or within organelles like mitochondria. Here we identify Vms1p as a tRNA hydrolase that releases stalled polypeptides engaged by the RQC.

Suggested Citation

  • Olga Zurita Rendón & Eric K. Fredrickson & Conor J. Howard & Jonathan Van Vranken & Sarah Fogarty & Neal D. Tolley & Raghav Kalia & Beatriz A. Osuna & Peter S. Shen & Christopher P. Hill & Adam Frost , 2018. "Vms1p is a release factor for the ribosome-associated quality control complex," Nature Communications, Nature, vol. 9(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04564-3
    DOI: 10.1038/s41467-018-04564-3
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    Cited by:

    1. Ji Geng & Shuangxi Li & Yu Li & Zhihao Wu & Sunil Bhurtel & Suman Rimal & Danish Khan & Rani Ohja & Onn Brandman & Bingwei Lu, 2024. "Stalled translation by mitochondrial stress upregulates a CNOT4-ZNF598 ribosomal quality control pathway important for tissue homeostasis," Nature Communications, Nature, vol. 15(1), pages 1-17, December.

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