ArticleCell cycle (Georgetown, Tex.)2016
Functional analysis of the uL11 protein impact on translational machinery.
Article in Cell cycle (Georgetown, Tex.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Translational resistance to amino acid starvation in breast cancer cells revealed by ribosome profiling.iScience · 2026Article
- Ribonuclease DIS3 delays aging and senescence by generating tRNA halves.Nature communications · 2026Article
- Disturbances in cell wall biogenesis as a key factor in the replicative aging of budding yeast.Biogerontology · 2025Article
- Phosphorylation of P-stalk proteins defines the ribosomal state for interaction with auxiliary protein factors.EMBO reports · 2024Article
- The flexible N-terminal motif of uL11 unique to eukaryotic ribosomes interacts with P-complex and facilitates protein translation.Nucleic acids research · 2022Article
- Single amino-acid mutation in a Drosoph ila melanogaster ribosomal protein: An insight in uL11 transcriptional activity.PloS one · 2022Article
- Structural impact of K63 ubiquitin on yeast translocating ribosomes under oxidative stress.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Ribosomal Protein uL11 as a Regulator of Metabolic Circuits Related to Aging and Cell Cycle.Cells · 2020Article
- Slowing ribosome velocity restores folding and function of mutant CFTR.The Journal of clinical investigation · 2019Article
- Article
- Multiplication of Ribosomal P-Stalk Proteins Contributes to the Fidelity of Translation.Molecular and cellular biology · 2017Article
- Human ribosomal P1-P2 heterodimer represents an optimal docking site for ricin A chain with a prominent role for P1 C-terminus.Scientific reports · 2017Article
- Placeholder factors in ribosome biogenesis: please, pave my way.Microbial cell (Graz, Austria) · 2017Review
- uL11, a central player in translation.Cell cycle (Georgetown, Tex.) · 2016Article
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ribosomal GTPase associated center constitutes the ribosomal area, which is the landing platform for translational GTPases and stimulates their hydrolytic activity. The ribosomal stalk represents a landmark structure in this center, and in eukaryotes is composed of uL11, uL10 and P1/P2 proteins. The modus operandi of the uL11 protein has not been exhaustively studied in vivo neither in prokaryotic nor in eukaryotic cells. Using a yeast model, we have brought functional insight into the translational apparatus deprived of uL11, filling the gap between structural and biochemical studies. We show that the uL11 is an important element in various aspects of 'ribosomal life'. uL11 is involved in 'birth' (biogenesis and initiation), by taking part in Tif6 release and contributing to ribosomal subunit-joining at the initiation step of translation. uL11 is particularly engaged in the 'active life' of the ribosome, in elongation, being responsible for the interplay with eEF1A and fidelity of translation and contributing to a lesser extent to eEF2-dependent translocation. Our results define the uL11 protein as a critical GAC element universally involved in trGTPase 'productive state' stabilization, being primarily a part of the ribosomal element allosterically contributing to the fidelity of the decoding event.
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