ArticleBiomolecules2023
Ribosomal Protein S12 Hastens Nucleation of Co-Transcriptional Ribosome Assembly.
Article in Biomolecules, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 9 citations in OpenAlex.
- Transcriptional Analysis of Cell Division-Related Genes inMicroorganisms · 2026Article
- Functional characterization of dynamic nascent RNA folding ensembles in real time.Science advances · 2026Article
- A comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation.Nucleic acids research · 2026Article
- Nascent RNA Folding and RNP Assembly Revealed by Single-molecule Microscopy.Journal of molecular biology · 2026Review
- pseudo-GhFAD2-1 Is a lncRNA Involved in Regulating Cottonseed Oleic and Linoleic Acid Ratios and Seed Size in Gossypium hirsutum.Plant biotechnology journal · 2025Article
- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Ribosomal subunits begin assembly during transcription of the ribosomal RNA (rRNA), when the rRNA begins to fold and associate with ribosomal proteins (RPs). In bacteria, the first steps of ribosome assembly depend upon recognition of the properly folded rRNA by primary assembly proteins such as S4, which nucleates assembly of the 16S 5' domain. Recent evidence, however, suggests that initial recognition by S4 is delayed due to variable folding of the rRNA during transcription. Here, using single-molecule colocalization co-transcriptional assembly (smCoCoA), we show that the late-binding RP S12 specifically promotes the association of S4 with the pre-16S rRNA during transcription, thereby accelerating nucleation of 30S ribosome assembly. Order of addition experiments suggest that S12 helps chaperone the rRNA during transcription, particularly near the S4 binding site. S12 interacts transiently with the rRNA during transcription and, consequently, a high concentration is required for its chaperone activity. These results support a model in which late-binding RPs moonlight as RNA chaperones during transcription in order to facilitate rapid assembly.
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Registered trials
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