5i2t

Publication Abstract from PubMed

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.

Pwp2 mediates UTP-B assembly via two structurally independent domains.,Boissier F, Schmidt CM, Linnemann J, Fribourg S, Perez-Fernandez J Sci Rep. 2017 Jun 9;7(1):3169. doi: 10.1038/s41598-017-03034-y. PMID:28600509^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.