ArticleRNA (New York, N.Y.)2005
The N-terminal extension of Escherichia coli ribosomal protein L20 is important for ribosome assembly, but dispensable for translational feedback control.
Article in RNA (New York, N.Y.), 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 21 citations in OpenAlex.
- Functional Analysis of BipA in E. coli Reveals the Natural Plasticity of 50S Subunit Assembly.Journal of molecular biology · 2020Article
- The eukaryote-specific N-terminal extension of ribosomal protein S31 contributes to the assembly and function of 40S ribosomal subunits.Nucleic acids research · 2016Article
- The extended loops of ribosomal proteins uL4 and uL22 of Escherichia coli contribute to ribosome assembly and protein translation.Nucleic acids research · 2016Article
- New shuttle vector-based expression system to generate polyhistidine-tagged fusion proteins in Staphylococcus aureus and Escherichia coli.Applied and environmental microbiology · 2015Article
- Deletion of L4 domains reveals insights into the importance of ribosomal protein extensions in eukaryotic ribosome assembly.RNA (New York, N.Y.) · 2014Article
- The N-terminal extension of S12 influences small ribosomal subunit assembly in Escherichia coli.RNA (New York, N.Y.) · 2014Article
- The role of disordered ribosomal protein extensions in the early steps of eubacterial 50 S ribosomal subunit assembly.International journal of molecular sciences · 2009Review
- Mutations in residues involved in zinc binding in the catalytic site of Escherichia coli threonyl-tRNA synthetase confer a dominant lethal phenotype.Journal of bacteriology · 2007Article
- Escherichia coli ribosomal protein L20 binds as a single monomer to its own mRNA bearing two potential binding sites.Nucleic acids research · 2007Article
- Ribosomal protein L20 controls expression of the Bacillus subtilis infC operon via a transcription attenuation mechanism.Nucleic acids research · 2007Article
- Coexistence of two protein folding states in the crystal structure of ribosomal protein L20.EMBO reports · 2006Article
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Escherichia coli autoregulatory ribosomal protein L20 consists of two structurally distinct domains. The C-terminal domain is globular and sits on the surface of the large ribosomal subunit whereas the N-terminal domain has an extended shape and penetrates deep into the RNA-rich core of the subunit. Many other ribosomal proteins have analogous internal or terminal extensions. However, the biological functions of these extended domains remain obscure. Here we show that the N-terminal tail of L20 is important for ribosome assembly in vivo. Indeed, a truncated version of L20 without its N-terminal tail is unable to complement the deletion of rplT, the gene encoding L20. In addition, this L20 truncation confers a lethal-dominant phenotype, suggesting that the N-terminal domain is essential for cell growth because it could be required for ribosome assembly. Supporting this hypothesis, partial deletions of the N-terminal tail of the protein are shown to cause a slow-growth phenotype due to altered ribosome assembly in vivo as large amounts of intermediate 40S ribosomal particles accumulate. In addition to being a ribosomal protein, L20 also acts as an autogenous repressor. Using L20 truncations, we also show that the N-terminal tail of L20 is dispensable for autogenous control.
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