ArticleThe Journal of biological chemistry
Rqc1 and other yeast proteins containing highly positively charged sequences are not targets of the RQC complex.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed.
- The ribosome-associated quality control factor TCF25 imposes K48 specificity on Listerin-mediated ubiquitination of nascent chains by binding and specifically orienting the acceptor ubiquitin.Genes & development · 2025Article
- Transcription factor 25 modulates gametocytogenesis and ribosome biogenesis in the malaria parasiteFrontiers in cellular and infection microbiology · 2025Article
- Massively parallel identification of sequence motifs triggering ribosome-associated mRNA quality control.Nucleic acids research · 2024Article
- Riboformer: a deep learning framework for predicting context-dependent translation dynamics.Nature communications · 2024Article
- Transcriptional profile of ribosome-associated quality control components and their associated phenotypes in mammalian cells.Scientific reports · 2024Article
- Expression and purification of soluble recombinant β-lactamases using Escherichia coli as expression host and pET-28a as cloning vector.Microbial cell factories · 2022Article
- Article
- Timer-based proteomic profiling of the ubiquitin-proteasome system reveals a substrate receptor of the GID ubiquitin ligase.Molecular cell · 2021Article
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8 authors.
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Abstract
Previous work has suggested that highly positively charged protein segments coded by rare codons or poly (A) stretches induce ribosome stalling and translational arrest through electrostatic interactions with the negatively charged ribosome exit tunnel, leading to inefficient elongation. This arrest leads to the activation of the Ribosome Quality Control (RQC) pathway and results in low expression of these reporter proteins. However, the only endogenous yeast proteins known to activate the RQC are Rqc1, a protein essential for RQC function, and Sdd1, a protein with unknown function, both of which contain polybasic sequences. To explore the generality of this phenomenon, we investigated whether the RQC complex controls the expression of other proteins with polybasic sequences. We showed by ribosome profiling data analysis and western blot that proteins containing polybasic sequences similar to, or even more positively charged than those of Rqc1 and Sdd1, were not targeted by the RQC complex. We also observed that the previously reported Ltn1-dependent regulation of Rqc1 is posttranslational, independent of the RQC activity. Taken together, our results suggest that RQC should not be regarded as a general regulatory pathway for the expression of highly positively charged proteins in yeast.
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