The Drosophila RNA binding protein Hrp48 binds a specific RNA sequence of the msl-2 mRNA 3' UTR to regulate translation
Language English Country Netherlands Media print-electronic
Document type Journal Article
PubMed
39504588
DOI
10.1016/j.bpc.2024.107346
PII: S0301-4622(24)00175-3
Knihovny.cz E-resources
- Keywords
- Dosage compensation, Hrp48, RNA binding protein, RNA recognition motif, Translation regulation,
- MeSH
- 3' Untranslated Regions * MeSH
- DNA-Binding Proteins MeSH
- Drosophila melanogaster * metabolism genetics MeSH
- Heterogeneous-Nuclear Ribonucleoproteins MeSH
- RNA, Messenger metabolism genetics chemistry MeSH
- Drosophila Proteins * metabolism chemistry genetics MeSH
- RNA-Binding Proteins * metabolism chemistry genetics MeSH
- Protein Biosynthesis MeSH
- Molecular Dynamics Simulation MeSH
- Transcription Factors metabolism chemistry genetics MeSH
- Protein Binding MeSH
- Binding Sites MeSH
- Animals MeSH
- Check Tag
- Animals MeSH
- Publication type
- Journal Article MeSH
- Names of Substances
- 3' Untranslated Regions * MeSH
- DNA-Binding Proteins MeSH
- Heterogeneous-Nuclear Ribonucleoproteins MeSH
- Hrb27C protein, Drosophila MeSH Browser
- RNA, Messenger MeSH
- msl-2 protein, Drosophila MeSH Browser
- Drosophila Proteins * MeSH
- RNA-Binding Proteins * MeSH
- Transcription Factors 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
References provided by Crossref.org
