ArticleNucleic acids research2014
Structural insights into the function of a unique tandem GTPase EngA in bacterial ribosome assembly.
Article in Nucleic acids research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 53 citations in OpenAlex.
- A Mechanistic Model of Cry2Ab12 Toxicity AgainstToxins · 2026Article
- Single-step in vitro reconstitution of theeLife · 2026Article
- Evolutionary Flexibility of Ribosome Biogenesis in Bacteria.Molecular biology and evolution · 2025Article
- Anti-sense oligonucleotide probing as a structural platform for studying ribonucleoprotein complex assembly.Nature communications · 2025Article
- Role of the sarcin-ricin loop of 23S rRNA in biogenesis of the 50S ribosomal subunit.RNA (New York, N.Y.) · 2025Article
- Protein bL38 facilitates incorporation of uL6 during assembly of the 50S subunit in Flavobacterium johnsoniae.Nucleic acids research · 2025Article
- The binding of RbgA to a critical 50S assembly intermediate facilitates YphC function in bacterial ribosomal assembly.Nucleic acids research · 2025Article
- YjgA plays dual roles in enhancing PTC maturation.Nucleic acids research · 2024Article
- Critical steps in the assembly process of the bacterial 50S ribosomal subunit.Nucleic acids research · 2024Review
- Domain consolidation in Bacterial 50S assembly revealed by Anti-Sense Oligonucleotide Probing.bioRxiv : the preprint server for biology · 2024Article
- Late consolidation of rRNA structure during co-transcriptional assembly inbioRxiv : the preprint server for biology · 2024Article
- Emerging Quantitative Biochemical, Structural, and Biophysical Methods for Studying Ribosome and Protein-RNA Complex Assembly.Biomolecules · 2023Review
- Characterizing a novel CMK-EngA fusion protein fromBiochemistry and biophysics reports · 2023Article
- Cryo-EM captures early ribosome assembly in action.Nature communications · 2023Article
- The ribosome assembly GTPase EngA is involved in redox signaling in cyanobacteria.Frontiers in microbiology · 2023Article
- Interconnected assembly factors regulate the biogenesis of mitoribosomal large subunit.The EMBO journal · 2021Article
- Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA.Frontiers in microbiology · 2021Article
- Structure of the mature kinetoplastids mitoribosome and insights into its large subunit biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Loss of a single methylation in 23S rRNA delays 50S assembly at multiple late stages and impairs translation initiation and elongation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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13 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Many ribosome-interacting GTPases, with proposed functions in ribosome biogenesis, are also implicated in the cellular regulatory coupling between ribosome assembly process and various growth control pathways. EngA is an essential GTPase in bacteria, and intriguingly, it contains two consecutive GTPase domains (GD), being one-of-a-kind among all known GTPases. EngA is required for the 50S subunit maturation. However, its molecular role remains elusive. Here, we present the structure of EngA bound to the 50S subunit. Our data show that EngA binds to the peptidyl transferase center (PTC) and induces dramatic conformational changes on the 50S subunit, which virtually returns the 50S subunit to a state similar to that of the late-stage 50S assembly intermediates. Very interestingly, our data show that the two GDs exhibit a pseudo-two-fold symmetry in the 50S-bound conformation. Our results indicate that EngA recognizes certain forms of the 50S assembly intermediates, and likely facilitates the conformational maturation of the PTC of the 23S rRNA in a direct manner. Furthermore, in a broad context, our data also suggest that EngA might be a sensor of the cellular GTP/GDP ratio, endowed with multiple conformational states, in response to fluctuations in cellular nucleotide pool, to facilitate and regulate ribosome assembly.
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