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

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 () and Jared Rutter ()
Additional contact information
Olga Zurita Rendón: Howard Hughes Medical Institute
Eric K. Fredrickson: University of Utah School of Medicine
Conor J. Howard: University of California, San Francisco
Jonathan Van Vranken: University of Utah School of Medicine
Sarah Fogarty: Howard Hughes Medical Institute
Neal D. Tolley: University of Utah
Raghav Kalia: University of Utah School of Medicine
Beatriz A. Osuna: 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
Jared Rutter: Howard Hughes Medical Institute

Nature Communications, 2018, vol. 9, issue 1, 1-9

Abstract: 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.

Date: 2018
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/s41467-018-04564-3 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-04564-3

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/s41467-018-04564-3

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().