Another layer of complexity in Staphylococcus aureus methionine biosynthesis control: unusual RNase III-driven T-box riboswitch cleavage determines met operon mRNA stability and decay
Zitieren Sie bitte immer diese URN: urn:nbn:de:bvb:20-opus-259029
- In Staphylococcus aureus, de novo methionine biosynthesis is regulated by a unique hierarchical pathway involving stringent-response controlled CodY repression in combination with a T-box riboswitch and RNA decay. The T-box riboswitch residing in the 5′ untranslated region (met leader RNA) of the S. aureus metICFE-mdh operon controls downstream gene transcription upon interaction with uncharged methionyl-tRNA. met leader and metICFE-mdh (m)RNAs undergo RNase-mediated degradation in a process whose molecular details are poorly understood. HereIn Staphylococcus aureus, de novo methionine biosynthesis is regulated by a unique hierarchical pathway involving stringent-response controlled CodY repression in combination with a T-box riboswitch and RNA decay. The T-box riboswitch residing in the 5′ untranslated region (met leader RNA) of the S. aureus metICFE-mdh operon controls downstream gene transcription upon interaction with uncharged methionyl-tRNA. met leader and metICFE-mdh (m)RNAs undergo RNase-mediated degradation in a process whose molecular details are poorly understood. Here we determined the secondary structure of the met leader RNA and found the element to harbor, beyond other conserved T-box riboswitch structural features, a terminator helix which is target for RNase III endoribonucleolytic cleavage. As the terminator is a thermodynamically highly stable structure, it also forms posttranscriptionally in met leader/ metICFE-mdh read-through transcripts. Cleavage by RNase III releases the met leader from metICFE-mdh mRNA and initiates RNase J-mediated degradation of the mRNA from the 5′-end. Of note, metICFE-mdh mRNA stability varies over the length of the transcript with a longer lifespan towards the 3′-end. The obtained data suggest that coordinated RNA decay represents another checkpoint in a complex regulatory network that adjusts costly methionine biosynthesis to current metabolic requirements.…
Autor(en): | Freya D. R WenckerORCiD, Gabriella MarincolaORCiD, Sonja M. K. SchoenfelderORCiD, Sandra MaaßORCiD, Dörte BecherORCiD, Wilma ZiebuhrORCiD |
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URN: | urn:nbn:de:bvb:20-opus-259029 |
Dokumentart: | Artikel / Aufsatz in einer Zeitschrift |
Institute der Universität: | Medizinische Fakultät / Institut für Molekulare Infektionsbiologie |
Sprache der Veröffentlichung: | Englisch |
Titel des übergeordneten Werkes / der Zeitschrift (Englisch): | Nucleic Acids Research |
Erscheinungsjahr: | 2021 |
Band / Jahrgang: | 49 |
Heft / Ausgabe: | 4 |
Seitenangabe: | 2192-2212 |
Originalveröffentlichung / Quelle: | Nucleic Acids Research (2021) 49:4, 2192-2212. https://doi.org/10.1093/nar/gkaa1277 |
DOI: | https://doi.org/10.1093/nar/gkaa1277 |
Allgemeine fachliche Zuordnung (DDC-Klassifikation): | 6 Technik, Medizin, angewandte Wissenschaften / 61 Medizin und Gesundheit / 610 Medizin und Gesundheit |
Freie Schlagwort(e): | acid; allelic replacement; antitermination; endoribonuclease; expression; geometry; mechanism; proteins; transcription; translation |
Datum der Freischaltung: | 05.05.2022 |
Sammlungen: | Open-Access-Publikationsfonds / Förderzeitraum 2021 |
Lizenz (Deutsch): | CC BY-NC: Creative-Commons-Lizenz: Namensnennung, Nicht kommerziell 4.0 International |