ArticleNucleic acids research2016
The extended loops of ribosomal proteins uL4 and uL22 of Escherichia coli contribute to ribosome assembly and protein translation.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- 23S rRNA modifications stimulate catalytic activity and prevent the formation of alternative structures.Nucleic acids research · 2026Article
- Cryo-EM reveals multiple mechanisms of ribosome inhibition by doxycycline.Nature communications · 2026Article
- Dual site targeting of the bacterial 70S ribosome by tetracyclines.Nature communications · 2026Article
- Remodelled ribosomal populations synthesize a specific proteome in proliferating plant tissue during cold.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2025Article
- The role of ribosomal protein networks in ribosome dynamics.Nucleic acids research · 2025Article
- Review
- Macrolide resistance through uL4 and uL22 ribosomal mutations in Pseudomonas aeruginosa.Nature communications · 2024Article
- Protein Fold Usages in Ribosomes: Another Glance to the Past.International journal of molecular sciences · 2024Article
- The Giardia lamblia ribosome structure reveals divergence in several biological pathways and the mode of emetine function.Structure (London, England : 1993) · 2024Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
- A Legionella toxin exhibits tRNA mimicry and glycosyl transferase activity to target the translation machinery and trigger a ribotoxic stress response.Nature cell biology · 2023Article
- Structural Consequences of Deproteinating the 50S Ribosome.Biomolecules · 2022Article
- Modulating co-translational protein folding by rational design and ribosome engineering.Nature communications · 2022Article
- Ribosomal protein eL39 is important for maturation of the nascent polypeptide exit tunnel and proper protein folding during translation.Nucleic acids research · 2022Article
- High-resolution structures of a thermophilic eukaryotic 80S ribosome reveal atomistic details of translocation.Nature communications · 2022Article
- A Survey of Spontaneous Antibiotic-Resistant Mutants of the Halophilic, Thermophilic BacteriumAntibiotics (Basel, Switzerland) · 2021Article
- A Novel Model for the RNase MRP-Induced Switch between the Formation of Different Forms of 5.8S rRNA.International journal of molecular sciences · 2021Article
- Evolution of ribosomal protein network architectures.Scientific reports · 2021Article
- Ribosome Purification from an α-proteobacterium and rRNA Analysis by Northern Blot.Bio-protocol · 2020Article
- Structural insights into assembly of the ribosomal nascent polypeptide exit tunnel.Nature communications · 2020Article
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6 authors.
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Abstract
Nearly half of ribosomal proteins are composed of a domain on the ribosome surface and a loop or extension that penetrates into the organelle's RNA core. Our previous work showed that ribosomes lacking the loops of ribosomal proteins uL4 or uL22 are still capable of entering polysomes. However, in those experiments we could not address the formation of mutant ribosomes, because we used strains that also expressed wild-type uL4 and uL22. Here, we have focused on ribosome assembly and function in strains in which loop deletion mutant genes are the ONLY: sources of uL4 or uL22 protein. The uL4 and uL22 loop deletions have different effects, but both mutations result in accumulation of immature particles that do not accumulate in detectable amounts in wild-type strains. Thus, our results suggest that deleting the loops creates kinetic barriers in the normal assembly pathway, possibly resulting in assembly via alternate pathway(s). Furthermore, deletion of the uL4 loop results in cold-sensitive ribosome assembly and function. Finally, ribosomes carrying either of the loop-deleted proteins responded normally to the secM translation pausing peptide, but the uL4 mutant responded very inefficiently to the cmlA(crb) pause peptide.
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