Jelena Jakovljevic

TL;DR: This work affinity purified yeast preribosomal particles containing the nucleolar protein Nop7p and developed means to separate their components, demonstrating that proteomic approaches in concert with genetic tools provide powerful means to purify and characterize ribosome assembly intermediates.

TL;DR: This work has identified a ribonucleoprotein neighborhood in preribosomes that contains two yeast ribosome assembly factors, Rpf2 and Rrs1, two ribosomal proteins, rpL5 and rPL11, and 5S rRNA, and interactions between each of these four proteins have been confirmed by binding assays in vitro.

TL;DR: Cryo-electron microscopy is used to characterize the structures of yeast nucleoplasmic pre-60S particles affinity-purified using the epitope-tagged assembly factor Nog2, and rich structural information in these structures provides a framework to dissect molecular roles of diverse assembly factors in eukaryotic ribosome assembly.

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 model provides an initial paradigm for the sequential assembly of eukaryotic 60S subunits and reveals striking differences and similarities between assembly of bacterial and eukARYotic large ribosomal subunits, providing insights into how these RNA-protein particles evolved.