Gisela Pöll

TL;DR: Comparative analysis of dynamic and steady-state maturation assays revealed that several r-proteins are required for efficient nuclear export of pre-18S rRNA, suggesting that they form an interaction platform with the export machinery.

TL;DR: The results show that key aspects of the assembly of eukaryotic r-proteins into distinct structural parts of the SSU are similar to the in vitro assembly pathway of their prokaryotic counterparts.

TL;DR: Working hypotheses are discussed on how individual r-proteins control the productive processing of the major 5′ end of 5.8S rRNA precursors by exonucleases Rat1p and Xrn1p, and the nature of structural characteristics of nascent LSUs that are required for cytoplasmic accumulation of nascent subunits but are nonessential for most of the nuclear LSU pre-rRNA processing events.

TL;DR: This work systematically investigated the assembly of large ribosomal subunit (LSU) r-proteins from the eukaryote S. cerevisiae and the impact of these proteins on the assembly states of other r-teins and on the transient LSU precursor association of several ribosome biogenesis factors, including Nog2, Rsa4 and Nop53 are discussed.

TL;DR: It is reported that rpS5 plays an additional local role at the head/platform interface in efficient SSU maturation and the suggested model can explain 18S precursor rRNA 3′ processing phenotypes observed in many eukaryotic SSU head assembly mutants.