Pwp2 mediates UTP-B assembly via two structurally independent domains.

The SSU processome constitutes a large ribonucleoprotein complex involved in the early steps of ribosome biogenesis. UTP-B is one of the first multi-subunit protein complexes that associates with the pre-ribosomal RNA to form the SSU processome. To understand the molecular basis of the hierarchical assembly of the SSU-processome, we have ...
undergone a structural and functional analysis of the UTP-B subunit Pwp2p. We show that Pwp2p is required for the proper assembly of UTP-B and for a productive association of UTP-B with pre-rRNA. These two functions are mediated by two distinct structural domains. The N-terminal domain of Pwp2p folds into a tandem WD-repeat (tWD) that associates with Utp21p, Utp18p, and Utp6p to form a core complex. The CTDs of Pwp2p and Utp21p mediate the assembly of the heterodimer Utp12p:Utp13p that is required for the stable incorporation of the UTP-B complex in the SSU processome. Finally, we provide evidence suggesting a role of UTP-B as a platform for the binding of assembly factors during the maturation of 20S rRNA precursors.
Mesh Terms:
Binding Sites, Cloning, Molecular, Escherichia coli, Gene Expression, Gene Expression Regulation, Fungal, Nuclear Proteins, Organelle Biogenesis, Phosphorylation, Protein Binding, Protein Conformation, alpha-Helical, Protein Conformation, beta-Strand, Protein Interaction Domains and Motifs, Protein Multimerization, RNA Precursors, RNA, Ribosomal, RNA-Binding Proteins, Recombinant Proteins, Ribosomal Proteins, Ribosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Sci Rep
Date: Dec. 09, 2016
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