The Drosophila RNA binding protein Hrp48 binds a specific RNA sequence of the msl-2 mRNA 3' UTR to regulate translation
Jazyk angličtina Země Nizozemsko Médium print-electronic
Typ dokumentu časopisecké články
PubMed
39504588
DOI
10.1016/j.bpc.2024.107346
PII: S0301-4622(24)00175-3
Knihovny.cz E-zdroje
- Klíčová slova
- Dosage compensation, Hrp48, RNA binding protein, RNA recognition motif, Translation regulation,
- MeSH
- 3' nepřekládaná oblast * MeSH
- DNA vazebné proteiny MeSH
- Drosophila melanogaster * metabolismus genetika MeSH
- heterogenní jaderné ribonukleoproteiny MeSH
- messenger RNA metabolismus genetika chemie MeSH
- proteiny Drosophily * metabolismus chemie genetika MeSH
- proteiny vázající RNA * metabolismus chemie genetika MeSH
- proteosyntéza MeSH
- simulace molekulární dynamiky MeSH
- transkripční faktory metabolismus chemie genetika MeSH
- vazba proteinů MeSH
- vazebná místa MeSH
- zvířata MeSH
- Check Tag
- zvířata MeSH
- Publikační typ
- časopisecké články MeSH
- Názvy látek
- 3' nepřekládaná oblast * MeSH
- DNA vazebné proteiny MeSH
- heterogenní jaderné ribonukleoproteiny MeSH
- Hrb27C protein, Drosophila MeSH Prohlížeč
- messenger RNA MeSH
- msl-2 protein, Drosophila MeSH Prohlížeč
- proteiny Drosophily * MeSH
- proteiny vázající RNA * MeSH
- transkripční faktory MeSH
Repression of msl-2 mRNA translation is essential for viability of Drosophila melanogaster females to prevent hypertranscription of both X chromosomes. This translational control event is coordinated by the female-specific protein Sex-lethal (Sxl) which recruits the RNA binding proteins Unr and Hrp48 to the 3' untranslated region (UTR) of the msl-2 transcript and represses translation initiation. The mechanism exerted by Hrp48 during translation repression and its interaction with msl-2 are not well understood. Here we investigate the RNA binding specificity and affinity of the tandem RNA recognition motifs of Hrp48. Using NMR spectroscopy, molecular dynamics simulations and isothermal titration calorimetry, we identified the exact region of msl-2 3' UTR recognized by Hrp48. Additional biophysical experiments and translation assays give further insights into complex formation of Hrp48, Unr, Sxl and RNA. Our results show that Hrp48 binds independent of Sxl and Unr downstream of the E and F binding sites of Sxl and Unr to msl-2.
Centre for Genomic Regulation 08003 Barcelona Spain
Department of Biochemistry 4 Biophysical Chemistry University of Bayreuth 95447 Bayreuth Germany
Molecular Systems Biology Unit European Molecular Biology Laboratory 69117 Heidelberg Germany
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