Yeast Ribosomal Protein L40 Assembles Late into Precursor 60 S Ribosomes and Is Required for Their Cytoplasmic Maturation

Fernández-Pévida, Antonio; Rodríguez-Galán, Olga; Díaz-Quintana, Antonio; Kressler, Dieter; Cruz, Jesús de la

doi:10.1074/jbc.m112.400564

Cited by 45 publications

(66 citation statements)

References 144 publications

(162 reference statements)

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“…In addition, the binding sites of L16 and L41e are not used by these proteins yet, but are instead occupied by rRNA helix 89 and helix 71, respectively. Also L40e appears to be absent, which is in agreement with a previous study showing that L40e, like L16 (refs 25,26), is assembled into the maturing 60S subunit only in the cytoplasm 27 .…”

Section: Resultssupporting

confidence: 92%

60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle

et al. 2014

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During eukaryotic ribosome biogenesis, nascent ribosomal RNA (rRNA) forms pre-ribosomal particles containing ribosomal proteins and assembly factors. Subsequently, these immature rRNAs are processed and remodelled. Little is known about the premature assembly states of rRNAs and their structural rearrangement during ribosome biogenesis. Using cryo-EM we characterize a pre-60S particle, where the 5S rRNA and its associated ribosomal proteins L18 and L5 (5S ribonucleoprotein (RNP)) are rotated by almost 180°when compared with the mature subunit. Consequently, neighbouring 25S rRNA helices that protrude from the base of the central protuberance are deformed. This altered topology is stabilized by nearby assembly factors (Rsa4 and Nog1), which were identified by fitting their three-dimensional structures into the cryo-EM density. We suggest that the 5S RNP performs a semicircular movement during 60S biogenesis to adopt its final position, fulfilling a chaperone-like function in guiding the flanking 25S rRNA helices of the central protuberance to their final topology.

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Section: Resultssupporting

confidence: 92%

60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle

et al. 2014

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“…Middle-acting r-proteins in turn are required for assembly of late-acting r-proteins (25, 26, 31, 104, 106, 108). A similar hierarchical dependence upon r-proteins for association of assembly factors with preribosomes was observed.…”

Section: Assembly Of 60s Ribosomal Subunitsmentioning

confidence: 99%

“…All but L24 are located on the subunit interface, adjacent to the CP, the PTC, and the GTPase-activating center (GAC). In the absence of L29 and L40 or upon depletion of L10, the LSU does not efficiently join to the SSUs (106, 129, 130). Thus, the last steps of LSU assembly are reserved for completion of active sites.…”

Section: Cytoplasmic Steps Of 60s Ribosomal Subunit Assemblymentioning

confidence: 99%

Functions of Ribosomal Proteins in Assembly of Eukaryotic Ribosomes In Vivo

Cruz

Karbstein

Woolford

2015

Annu. Rev. Biochem.

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The proteome of cells is synthesized by ribosomes, complex ribonucleoproteins that in eukaryotes contain 79–80 proteins and four ribosomal RNAs (rRNAs) more than 5,400 nucleotides long. How these molecules assemble together and how their assembly is regulated in concert with the growth and proliferation of cells remain important unanswered questions. Here, we review recently emerging principles to understand how eukaryotic ribosomal proteins drive ribosome assembly in vivo. Most ribosomal proteins assemble with rRNA cotranscriptionally; their association with nascent particles is strengthened as assembly proceeds. Each subunit is assembled hierarchically by sequential stabilization of their subdomains. The active sites of both subunits are constructed last, perhaps to prevent premature engagement of immature ribosomes with active subunits. Late-assembly intermediates undergo quality-control checks for proper function. Mutations in ribosomal proteins that affect mostly late steps lead to ribosomopathies, diseases that include a spectrum of cell type–specific disorders that often transition from hypoproliferative to hyperproliferative growth.

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“…The segregation of large subunits into distinct structural domains is not as apparent as for small subunits (Ban et al 2000); the six rRNA domains are more intertwined in large subunits (Holbrook 2008). Hence, it was initially striking to find that depletion of individual yeast large subunit RPs (RPLs) led to specific rather than global pre-rRNA processing defects (Ferreira-Cerca et al 2005;Hofer et al 2007;Robledo et al 2008;Poll et al 2009; Fernandez-Pevida et al 2012;Jakovljevic et al 2012;Gamalinda et al 2013), which are grouped into early, middle, and late classes (Table 1). From these results, we observed a pattern previously not described: RPLs belonging to these phenotypic classes are remarkably clustered into distinct structural neighborhoods of the yeast 60S subunit ( Fig.…”

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confidence: 99%

A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains

et al. 2014

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Despite having high-resolution structures for eukaryotic large ribosomal subunits, it remained unclear how these ribonucleoprotein complexes are constructed in living cells. Nevertheless, knowing where ribosomal proteins interact with ribosomal RNA (rRNA) provides a strategic platform to investigate the connection between spatial and temporal aspects of 60S subunit biogenesis. We previously found that the function of individual yeast large subunit ribosomal proteins (RPLs) in precursor rRNA (pre-rRNA) processing correlates with their location in the structure of mature 60S subunits. This observation suggested that there is an order by which 60S subunits are formed. To test this model, we used proteomic approaches to assay changes in the levels of ribosomal proteins and assembly factors in preribosomes when RPLs functioning in early, middle, and late steps of pre-60S assembly are depleted. Our results demonstrate that structural domains of eukaryotic 60S ribosomal subunits are formed in a hierarchical fashion. Assembly begins at the convex solvent side, followed by the polypeptide exit tunnel, the intersubunit side, and finally the central protuberance. This model provides an initial paradigm for the sequential assembly of eukaryotic 60S subunits. Our results reveal striking differences and similarities between assembly of bacterial and eukaryotic large ribosomal subunits, providing insights into how these RNA-protein particles evolved.

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Yeast Ribosomal Protein L40 Assembles Late into Precursor 60 S Ribosomes and Is Required for Their Cytoplasmic Maturation

Cited by 45 publications

References 144 publications

60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle

60S ribosome biogenesis requires rotation of the 5S ribonucleoprotein particle

Functions of Ribosomal Proteins in Assembly of Eukaryotic Ribosomes In Vivo

A hierarchical model for assembly of eukaryotic 60S ribosomal subunit domains

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