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• W169042602 abstract "The eukaryotic ribosome of baker's yeast (Saccharomyces cerevisiae) consists of two subunits, comprised in total of 79 ribosomal proteins (r-proteins) and four different ribosomal RNA (rRNA) species. Bringing these components together is a very complicated process in vivo involving more than 70 small nucleolar RNAs (snoRNAs) and around 150 accessory proteins. Nevertheless, the cell fulfils this challenge in a highly efficient manner. Although homologies with known protein motifs exist for some of these biogenesis factors, the exact function of these as well as for the majority of the remaining factors remains elusive. One early aspect of eukaryotic ribosome biogenesis is the co-transcriptional assembly of the small subunit (SSU) processome. This ribonucleoprotein (RNP) particle is required for early pre-rRNA processing events, separating the maturation of the SSU from the one of the large subunit (LSU). This process involves about 40 proteins, which are all required for SSU maturation and can be classified into five subgroups. Members of four of these subgroups have been shown to exist as entities in the cell independent of their interaction with pre-ribosomes.The goal of this work was to investigate the relationship between SSU r-protein and SSU processome assembly. To this end, representative r-proteins of all three major structural domains of the SSU rRNA were conditionally depleted in different Saccharomyces cerevisiae strains. Subsequently, the association of representatives of each subgroup of the SSU processome to early pre-ribosomes was analysed by complementary techniques. Among them, a mass spectrometry based method allowing the semiquantitative comparison of the protein composition of affinity purified pre-ribosomal particles was established and successfully applied. In comparison to earlier reports, more than twice the amount of proteins could be identified in these proteomic analyses of early pre-ribosomes, emphasizing the sensitivity of the established assay. Additionally, the obtained proteomic data provide evidence that factors required for maturation of the LSU are associated with these early pre-ribosomes, although in general less stable than their counterparts required for SSU maturation. Apart from this, the results obtained by this combined approach indicate that assembly of the SSU processome UTP-A, UTP-B and Mpp10p submodules with pre-rRNA can proceed independent of r-protein assembly events. This suggests that proteins, belonging to these subclasses, assist in proper primary rRNA folding events, potentially by preventing erroneous folding and thus providing binding sites for subsequent r-protein binding. In this regard, these proteins might be envisioned to function in a “chaperone like” way, dedicated to early pre-rRNAs. In contrast, efficient association of other SSU processome components, e.g. Noc4p or the SSU processome UTP-C submodule, with pre-ribosomes requires specific r-protein assembly events in the SSU rRNA central and 3’ domain. Moreover, the results point towards a function of Noc4p in the coordination of SSU rRNA central and 3’ domain assembly. Accordingly, establishment of a defined central domain assembly state is required for efficient Noc4p association with early pre-ribosomes and subsequently Noc4p is required to trigger assembly events in the SSU rRNA 3’ domain leading to a mature SSU head structure.Altogether, the data obtained in this work give a first comprehensive picture of the interplay between early steps in r-protein and SSU processome assembly with pre-rRNA in yeast cells." @default.
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• W169042602 date "2011-01-18" @default.
• W169042602 modified "2023-09-27" @default.
• W169042602 title "Analysis of the relationship between ribosomal protein and SSU processome assembly in Saccharomyces cerevisiae" @default.
• W169042602 hasPublicationYear "2011" @default.
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