9EN7
Hrp48 RRM1 domain
Summary for 9EN7
Entry DOI | 10.2210/pdb9en7/pdb |
Descriptor | Heterogeneous nuclear ribonucleoprotein 27C, GLYCEROL (3 entities in total) |
Functional Keywords | rna-recognition motif, rrm, translational control, rna binding protein |
Biological source | Drosophila melanogaster (fruit fly) |
Total number of polymer chains | 1 |
Total formula weight | 10286.44 |
Authors | Lomoschitz, A.,Hennig, J.,Murciano, B.,Meyer, J. (deposition date: 2024-03-12, release date: 2024-11-13, Last modification date: 2024-11-20) |
Primary citation | Lomoschitz, A.,Meyer, J.,Guitart, T.,Krepl, M.,Lapouge, K.,Hayn, C.,Schweimer, K.,Simon, B.,Sponer, J.,Gebauer, F.,Hennig, J. The Drosophila RNA binding protein Hrp48 binds a specific RNA sequence of the msl-2 mRNA 3' UTR to regulate translation. Biophys.Chem., 316:107346-107346, 2024 Cited by PubMed Abstract: 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. PubMed: 39504588DOI: 10.1016/j.bpc.2024.107346 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.19 Å) |
Structure validation
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