Ornithine capture by a translating ribosome controls bacterial polyamine synthesis
| Autor: | Alba Herrero del Valle, C. Axel Innis, Britta Seip, Guénaël Sacheau, Iñaki Cervera-Marzal, A. Carolin Seefeldt |
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| Rok vydání: | 2020 |
| Předmět: |
Microbiology (medical)
Models Molecular Ornithine Salmonella typhimurium Immunology Ornithine Decarboxylase Applied Microbiology and Biotechnology Microbiology Ribosome Article Ornithine decarboxylase 03 medical and health sciences chemistry.chemical_compound Bacterial Proteins RNA Transfer Genetics Protein biosynthesis Enterococcus faecalis Escherichia coli Polyamines Protein Interaction Domains and Motifs Amino Acid Sequence Phylogeny 030304 developmental biology 0303 health sciences Binding Sites Base Sequence Sequence Homology Amino Acid Virulence 030306 microbiology Chemistry Effector Thermus thermophilus Translation (biology) Cell Biology Cell biology Transcription antitermination Protein Biosynthesis Release factor Polyamine Ribosomes Sequence Alignment Peptide Termination Factors Protein Binding |
| Zdroj: | Nature Microbiology Nature microbiology |
| ISSN: | 2058-5276 |
| DOI: | 10.1038/s41564-020-0669-1 |
| Popis: | Polyamines are essential metabolites that play an important role in cell growth, stress adaptation, and microbial virulence1–3. In order to survive and multiply within a human host, pathogenic bacteria adjust the expression and activity of polyamine biosynthetic enzymes in response to different environmental stresses and metabolic cues2. Here, we show that ornithine capture by the ribosome and the nascent peptide SpeFL controls polyamine synthesis in γ-proteobacteria by inducing the expression of the ornithine decarboxylase SpeF4, via a mechanism involving ribosome stalling and transcription antitermination. In addition, we present the cryo-EM structure of an Escherichia coli (E. coli) ribosome stalled during translation of speFL in the presence of ornithine. The structure shows how the ribosome and the SpeFL sensor domain form a highly selective binding pocket that accommodates a single ornithine molecule but excludes near-cognate ligands. Ornithine pre-associates with the ribosome and is then held in place by the sensor domain, leading to the compaction of the SpeFL effector domain and blocking the action of release factor RF1. Thus, our study not only reveals basic strategies by which nascent peptides assist the ribosome in detecting a specific metabolite, but also provides a framework for assessing how ornithine promotes virulence in several human pathogens. |
| Databáze: | OpenAIRE |
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