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Ornithine capture by a translating ribosome controls bacterial polyamine synthesis

View ORCID ProfileAlba Herrero del Valle, View ORCID ProfileBritta Seip, Iñaki Cervera-Marzal, Guénaël Sacheau, View ORCID ProfileA. Carolin Seefeldt, View ORCID ProfileC. Axel Innis
doi: https://doi.org/10.1101/604074
Alba Herrero del Valle
1Institut Européen de Chimie et Biologie, Univ. Bordeaux, Institut National de la Santé et de la Recherche Médicale (U1212) and Centre National de la Recherche Scientifique (UMR 5320), Pessac 33607, France
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Britta Seip
1Institut Européen de Chimie et Biologie, Univ. Bordeaux, Institut National de la Santé et de la Recherche Médicale (U1212) and Centre National de la Recherche Scientifique (UMR 5320), Pessac 33607, France
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Iñaki Cervera-Marzal
1Institut Européen de Chimie et Biologie, Univ. Bordeaux, Institut National de la Santé et de la Recherche Médicale (U1212) and Centre National de la Recherche Scientifique (UMR 5320), Pessac 33607, France
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Guénaël Sacheau
1Institut Européen de Chimie et Biologie, Univ. Bordeaux, Institut National de la Santé et de la Recherche Médicale (U1212) and Centre National de la Recherche Scientifique (UMR 5320), Pessac 33607, France
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A. Carolin Seefeldt
1Institut Européen de Chimie et Biologie, Univ. Bordeaux, Institut National de la Santé et de la Recherche Médicale (U1212) and Centre National de la Recherche Scientifique (UMR 5320), Pessac 33607, France
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C. Axel Innis
1Institut Européen de Chimie et Biologie, Univ. Bordeaux, Institut National de la Santé et de la Recherche Médicale (U1212) and Centre National de la Recherche Scientifique (UMR 5320), Pessac 33607, France
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  • For correspondence: axel.innis@inserm.fr
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ABSTRACT

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 bacterial polyamine synthesis 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 specific metabolites, but also provides a framework for assessing how ornithine promotes virulence in several human pathogens.

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The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY-NC-ND 4.0 International license.
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Posted April 09, 2019.
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Ornithine capture by a translating ribosome controls bacterial polyamine synthesis
Alba Herrero del Valle, Britta Seip, Iñaki Cervera-Marzal, Guénaël Sacheau, A. Carolin Seefeldt, C. Axel Innis
bioRxiv 604074; doi: https://doi.org/10.1101/604074
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Ornithine capture by a translating ribosome controls bacterial polyamine synthesis
Alba Herrero del Valle, Britta Seip, Iñaki Cervera-Marzal, Guénaël Sacheau, A. Carolin Seefeldt, C. Axel Innis
bioRxiv 604074; doi: https://doi.org/10.1101/604074

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