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  An Hfq-dependent post-transcriptional mechanism fine tunes RecB expression in Escherichia coli

Kalita, I., Iosub, I. A., McLaren, L., Goossens, L., Granneman, S., & Karoui, M. E. (2023). An Hfq-dependent post-transcriptional mechanism fine tunes RecB expression in Escherichia coli. bioRxiv: the preprint server for biology, 2021.10.23.465540.

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Datensatz-Permalink: https://hdl.handle.net/21.11116/0000-000D-FDB5-A Versions-Permalink: https://hdl.handle.net/21.11116/0000-000F-3DF3-B
Genre: Preprint

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https://doi.org/10.1101/2021.10.23.465540 (Preprint)
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 Urheber:
Kalita, Irina1, Autor
Iosub, Ira Alexandra2, Autor
McLaren, Lorna2, Autor
Goossens, Louise2, Autor
Granneman, Sander2, Autor
Karoui, Meriem El2, Autor
Affiliations:
1Max Planck Institute for Terrestrial Microbiology_others, Max Planck Institute for Terrestrial Microbiology, Max Planck Society, Karl-von Frisch Str. 10, 35043 Marburg, Germany, ou_3556424              
2external, ou_persistent22              

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 Zusammenfassung: All living organisms have developed strategies to respond to chromosomal damage and preserve genome integrity. One such response is the repair of DNA double-strand breaks (DSBs), one of the most toxic forms of DNA lesions. In Escherichia coli, DSBs are repaired via RecBCD-dependent homologous recombination. RecBCD is essential for accurate chromosome maintenance, but its over-expression can lead to reduced DNA repair ability. This apparent paradox suggests that RecBCD copy numbers may need to be tightly controlled within an optimal range. Using single-molecule fluorescence mi-croscopy, we have established that RecB is present in very low abundance at mRNA and protein levels. RecB transcription shows high fluctuations, yet cell-to-cell protein variability remains remarkably low. Here, we show that the post-transcriptional regulator Hfq binds to recB mRNA and down-regulates RecB protein translation in vivo. Furthermore, specific disruption of the Hfq-binding site leads to more efficient translation of recB mRNAs. In addition, we observe a less effective reduction of RecB protein fluctuations in the absence of Hfq. This fine-tuning Hfq-mediated mechanism might have the underlying physiological function of maintaining RecB protein levels within an optimal range.Competing Interest StatementThe authors have declared no competing interest.

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Sprache(n): eng - English
 Datum: 2023-11-24
 Publikationsstatus: Erschienen
 Seiten: -
 Ort, Verlag, Ausgabe: -
 Inhaltsverzeichnis: -
 Art der Begutachtung: Keine Begutachtung
 Identifikatoren: URI: http://biorxiv.org/content/early/2023/11/24/2021.10.23.465540.abstract
DOI: 10.1101/2021.10.23.465540
bioRxiv: 10.1101/2021.10.23.465540
 Art des Abschluß: -

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Titel: bioRxiv : the preprint server for biology
  Kurztitel : bioRxiv
Genre der Quelle: Zeitschrift
 Urheber:
Affiliations:
Ort, Verlag, Ausgabe: -
Seiten: - Band / Heft: - Artikelnummer: 2021.10.23.465540 Start- / Endseite: - Identifikator: ZDB: 2766415-6
CoNE: https://pure.mpg.de/cone/journals/resource/2766415-6