RIP-Seq suggests translational regulation by L7Ae in Archaea
Abstract: L7Ae is a universal archaeal protein that recognizes and stabilizes kink-turn (k-turn) motifs in RNA substrates. These structural motifs are widespread in na-ture and are found in many functional RNA species, including ribosomal RNAs. Syn-thetic biology approaches utilize L7Ae/k-turn interactions to control gene expressionin eukaryotes. Here, we present results of comprehensive RNA immunoprecipitationsequencing (RIP-Seq) analysis of genomically tagged L7Ae from the hyperthermo-philic archaeonSulfolobus acidocaldarius. A large set of interacting noncoding RNAswas identified. In addition, several mRNAs, including thel7aetranscript, were foundto contain k-turn motifs that facilitate L7Ae binding.In vivostudies showed thatL7Ae autoregulates the translation of its mRNA by binding to a k-turn motif presentin the 5=untranslated region (UTR). A green fluorescent protein (GFP) reporter sys-tem was established inEscherichia coliand verified conservation of L7Ae-mediatedfeedback regulation inArchaea. Mobility shift assays confirmed binding to a k-turnin the transcript ofnop5-fibrillarin, suggesting that the expression of all C/D boxsRNP core proteins is regulated by L7Ae. These studies revealed that L7Ae-mediatedgene regulation evolved in archaeal organisms, generating new tools for the modu-lation of synthetic gene circuits in bacteria
- Standort
-
Deutsche Nationalbibliothek Frankfurt am Main
- Umfang
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Online-Ressource
- Sprache
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Englisch
- Anmerkungen
-
mBio. - 8, 4 (2017) , e00730-17, ISSN: 2150-7511
- Ereignis
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Veröffentlichung
- (wo)
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Freiburg
- (wer)
-
Universität
- (wann)
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2019
- Urheber
- DOI
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10.1128/mbio.00730-17
- URN
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urn:nbn:de:bsz:25-freidok-1438360
- Rechteinformation
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Kein Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Letzte Aktualisierung
-
14.08.2025, 10:58 MESZ
Datenpartner
Deutsche Nationalbibliothek. Bei Fragen zum Objekt wenden Sie sich bitte an den Datenpartner.
Beteiligte
- Daume, Michael
- Uhl, Michael
- Backofen, Rolf
- Randau, Lennart
- Universität
Entstanden
- 2019
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