ArticleThe EMBO journal2023
Structure of a bacterial ribonucleoprotein complex central to the control of cell envelope biogenesis.
Article in The EMBO journal, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed.
- Identification of proteins interacting with the N-terminal half of endoribonuclease RNase E inRNA biology · 2026Article
- Bacterial small regulatory RNAs.Nature reviews. Microbiology · 2026Review
- Multilevel Regulation of Peptidoglycan Dynamics in Bacteria: From Molecular Mechanisms to Applied Perspectives.Biomolecules · 2026Review
- Cooperation of regulatory RNA and the RNA degradosome in transcript surveillance.Nucleic acids research · 2024Article
- What goes up must come down: off switches for regulatory RNAs.Genes & development · 2024Review
- Evaluation of 5'-End Phosphorylation for Small RNA Stability and Target Regulation In Vivo.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Role of the 5' end phosphorylation state for small RNA stability and target RNA regulation in bacteria.Nucleic acids research · 2023Article
- Recent Advances in Peptidoglycan Synthesis and Regulation in Bacteria.Biomolecules · 2023Review
- Structure of a bacterial ribonucleoprotein complex central to the control of cell envelope biogenesis.The EMBO journal · 2023Article
Corrections and comments
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Authors and funding
7 authors.
Funding
Abstract
Biogenesis of the essential precursor of the bacterial cell envelope, glucosamine-6-phosphate (GlcN6P), is controlled by intricate post-transcriptional networks mediated by GlmZ, a small regulatory RNA (sRNA). GlmZ stimulates translation of the mRNA encoding GlcN6P synthtase in Escherichia coli, but when bound by RapZ protein, the sRNA becomes inactivated through cleavage by the endoribonuclease RNase E. Here, we report the cryoEM structure of the RapZ:GlmZ complex, revealing a complementary match of the RapZ tetrameric quaternary structure to structural repeats in the sRNA. The nucleic acid is contacted by RapZ mostly through a highly conserved domain that shares an evolutionary relationship with phosphofructokinase and suggests links between metabolism and riboregulation. We also present the structure of a precleavage intermediate formed between the binary RapZ:GlmZ complex and RNase E that reveals how GlmZ is presented and recognised by the enzyme. The structures provide a framework for understanding how other encounter complexes might guide recognition and action of endoribonucleases on target transcripts, and how structured substrates in polycistronic precursors may be recognised for processing by RNase E.
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Registered trials
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.