Download MendeleyStructural basis for 5'-ETS recognition by Utp4 at the early stages of ribosome biogenesis.
Calvino, F.R., Kornprobst, M., Schermann, G., Birkle, F., Wild, K., Fischer, T., Hurt, E., Ahmed, Y.L., Sinning, I.(2017) PLoS One 12: e0178752-e0178752
- PubMed: 28575120
- DOI: https://doi.org/10.1371/journal.pone.0178752
- Primary Citation of Related Structures:
5N1A - PubMed Abstract:
Eukaryotic ribosome biogenesis begins with the co-transcriptional assembly of the 90S pre-ribosome. The 'U three protein' (UTP) complexes and snoRNP particles arrange around the nascent pre-ribosomal RNA chaperoning its folding and further maturation. The earliest event in this hierarchical process is the binding of the UTP-A complex to the 5'-end of the pre-ribosomal RNA (5'-ETS). This oligomeric complex predominantly consists of β-propeller and α-solenoidal proteins. Here we present the structure of the Utp4 subunit from the thermophilic fungus Chaetomium thermophilum at 2.15 Å resolution and analyze its function by UV RNA-crosslinking (CRAC) and in context of a recent cryo-EM structure of the 90S pre-ribosome. Utp4 consists of two orthogonal and highly basic β-propellers that perfectly fit the EM-data. The Utp4 structure highlights an unusual Velcro-closure of its C-terminal β-propeller as relevant for protein integrity and potentially Utp8 recognition in the context of the pre-ribosome. We provide a first model of the 5'-ETS RNA from the internally hidden 5'-end up to the region that hybridizes to the 3'-hinge sequence of U3 snoRNA and validate a specific Utp4/5'-ETS interaction by CRAC analysis.
Organizational Affiliation:
Heidelberg University Biochemistry Center (BZH), Im Neuenheimer Feld 328, Heidelberg, Germany.
