ArticleMolecular cell2008
Structural and functional analysis of the E. coli NusB-S10 transcription antitermination complex.
Article in Molecular cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 115 citations in OpenAlex.
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- Extraribosomal Functions of Bacterial Ribosomal Proteins-An Update, 2023.International journal of molecular sciences · 2024Review
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- Ligand-Based Drug Design of Novel Antimicrobials againstInternational journal of molecular sciences · 2022Article
- Transcription complexes as RNA chaperones.Transcription · 2021Article
- Modulators of protein-protein interactions as antimicrobial agents.RSC chemical biology · 2021Review
- Effects of Ribosomal Protein S10 Flexible Loop Mutations on Tetracycline and Tigecycline Susceptibility ofFrontiers in microbiology · 2021Article
- Overproduction of a Dominant Mutant of the Conserved Era GTPase Inhibits Cell Division in Escherichia coli.Journal of bacteriology · 2020Article
- Escherichia coli NusG Links the Lead Ribosome with the Transcription Elongation Complex.iScience · 2020Article
- Nusbiarylins Inhibit Transcription and Target Virulence Factors in Bacterial PathogenInternational journal of molecular sciences · 2020Article
- How to choose templates for modeling of protein complexes: Insights from benchmarking template-based docking.Proteins · 2020Article
- RNA Polymerase's Relationship with the Ribosome: Not So Physical, Most of the Time.Journal of molecular biology · 2020Review
- NusA directly interacts with antitermination factor Q from phage λ.Scientific reports · 2020Article
- Identification of Functional Interactome of Colistin Resistance Protein MCR-1 inFrontiers in microbiology · 2020Article
- Deficiency of mitoribosomal S10 protein affects translation and splicing in Arabidopsis mitochondria.Nucleic acids research · 2019Article
- Structural basis for the function of SuhB as a transcription factor in ribosomal RNA synthesis.Nucleic acids research · 2019Article
- SuhB is an integral part of the ribosomal antitermination complex and interacts with NusA.Nucleic acids research · 2019Article
- Reversible fold-switching controls the functional cycle of the antitermination factor RfaH.Nature communications · 2019Article
1 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
Protein S10 is a component of the 30S ribosomal subunit and participates together with NusB protein in processive transcription antitermination. The molecular mechanisms by which S10 can act as a translation or a transcription factor are not understood. We used complementation assays and recombineering to delineate regions of S10 dispensable for antitermination, and determined the crystal structure of a transcriptionally active NusB-S10 complex. In this complex, S10 adopts the same fold as in the 30S subunit and is blocked from simultaneous association with the ribosome. Mass spectrometric mapping of UV-induced crosslinks revealed that the NusB-S10 complex presents an intermolecular, composite, and contiguous binding surface for RNAs containing BoxA antitermination signals. Furthermore, S10 overproduction complemented a nusB null phenotype. These data demonstrate that S10 and NusB together form a BoxA-binding module, that NusB facilitates entry of S10 into the transcription machinery, and that S10 represents a central hub in processive antitermination.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.