Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy

Greber, B.J.

doi:10.1261/rna.057927.116

Cited by 58 publications

(69 citation statements)

References 190 publications

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“…Interestingly, as shown by high-resolution cryo-EM, Rei1 and the closely related Reh1 probe the exit tunnel in a manner similar to Nog1 [25,28,30]. During P-stalk assembly, recruitment of uL10 is coupled with the release of Yvh1, which has previously displaced Mrt4 from pre-60S particles [103,104]. Release of the export adaptor Nmd3 is promoted by the GTPase Lsg1 and connected to the stable incorporation of uL16 [40,103,107] (Figure 2Q).…”

Section: Assembly Of the Lsumentioning

confidence: 89%

“…Nuclear Export and Cytoplasmic Maturation of Pre-60S Ribosomes Several export-mediating factors interact with different surfaces of pre-60S ribosomes to mediate their efficient translocation across the NPC [5,10,14,103] (Figures 2O and 5). Following the release of Nog2, the export adaptor Nmd3 binds in the A-, P-, and E-tRNA-binding sites of the LSU and recruits the exportin Crm1/Xpo1 via its essential NES sequences [10,14,30,32,101].…”

Section: Assembly Of the Lsumentioning

confidence: 99%

“…A recent study has demonstrated that recruitment and release of Mex67-Mtr2 is also intimately coupled to maturation of the emerging P stalk [104]. Besides these, several additional factors contribute to the export process [5,10,14,103], most likely by shielding the charged ribosomal surface against the hydrophobic environment within the NPC channel.…”

Section: Assembly Of the Lsumentioning

confidence: 99%

“…After export, removal of the remaining biogenesis factors is coordinated with the incorporation of the missing r-proteins [5,6,14,30,103] (Figure 2P). First, the AAA-ATPase Drg1 releases the GTPase Nog1 and its binding partner Rlp24, thereby enabling recruitment of the r-protein eL24 [99,106].…”

Section: Assembly Of the Lsumentioning

confidence: 99%

“…First, the AAA-ATPase Drg1 releases the GTPase Nog1 and its binding partner Rlp24, thereby enabling recruitment of the r-protein eL24 [99,106]. Subsequently, Arx1 is dissociated by Jjj1 and Rei1 [103]. Interestingly, as shown by high-resolution cryo-EM, Rei1 and the closely related Reh1 probe the exit tunnel in a manner similar to Nog1 [25,28,30].…”

Section: Assembly Of the Lsumentioning

confidence: 99%

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A Puzzle of Life: Crafting Ribosomal Subunits

Kressler

Hurt

Baßler

2017

Trends in Biochemical Sciences

163

127

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The biogenesis of eukaryotic ribosomes is a complicated process during which the transcription, modification, folding, and processing of the rRNA is coupled with the ordered assembly of $80 ribosomal proteins (r-proteins). Ribosome synthesis is catalyzed and coordinated by more than 200 biogenesis factors as the preribosomal subunits acquire maturity on their path from the nucleolus to the cytoplasm. Several biogenesis factors also interconnect the progression of ribosome assembly with quality control of important domains, ensuring that only functional subunits engage in translation. With the recent visualization of several assembly intermediates by cryoelectron microscopy (cryo-EM), a structural view of ribosome assembly begins to emerge. In this review we integrate these first structural insights into an updated overview of the consecutive ribosome assembly steps. Synopsis of Eukaryotic Ribosome AssemblyRibosomes are the molecular machines that translate the genetic information from the intermediary mRNA templates into proteins [1]. Eukaryotic 80S ribosomes comprise two unequal subunits that contain four different rRNAs and around 80 r-proteins ( Figure 1). The small 40S subunit (SSU) comprises the 18S rRNA and 33 r-proteins (referred to as RPS or S). The large 60S subunit (LSU) comprises the 25S/28S, 5.8S, and 5S rRNA and, in most eukaryotic species, 47 r-proteins (RPL or L); a notable exception is budding yeasts, which lack eL28The act of building a ribosome begins in the nucleolus, where the ribosomal DNA (rDNA) is transcribed into a long pre-rRNA precursor (35S pre-rRNA in yeast) and involves the ordered assembly of the r-proteins with the pre-rRNA, which is concomitantly processed into the mature rRNA species [5][6][7][8] (Figure 1 and Box 1). These assembly and processing events are tightly coupled and occur within preribosomal particles (see Glossary) that travel, as maturation progresses, from the nucleus across nuclear pore complexes (NPCs) to the cytoplasm, where they are ultimately converted into translation-competent ribosomal subunits [5,[9][10][11][12][13] (Figure 2, Key Figure). Given the gargantuan complexity of this process, it is unsurprising that the assembly of eukaryotic ribosomes strictly requires the assistance of a plethora (>200) of mostly essential ribosome biogenesis factors, which are also called trans-acting or assembly factors [5,14,15].Our current knowledge has been mainly obtained by studying ribosome biogenesis in the yeast Saccharomyces cerevisiae. Research conducted in the 1970s defined the r-protein composition of ribosomes, revealed the major pre-rRNA processing intermediates, and uncovered the existence of the 90S, 43S, and 66S preribosomal particles. The following 25 years witnessed the identification of numerous biogenesis factors and attributed functional roles TrendsCryoelectron microscopy analyses of the 90S preribosome show that the biogenesis factors create a casting mold that encloses the nascent pre-40S subunit.Structures of nuclear pre-60S particles reveal that a...

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Section: Assembly Of the Lsumentioning

confidence: 89%

Section: Assembly Of the Lsumentioning

confidence: 99%

Section: Assembly Of the Lsumentioning

confidence: 99%

Section: Assembly Of the Lsumentioning

confidence: 99%

Section: Assembly Of the Lsumentioning

confidence: 99%

See 3 more Smart Citations

A Puzzle of Life: Crafting Ribosomal Subunits

Kressler

Hurt

Baßler

2017

Trends in Biochemical Sciences

163

127

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Wide mutational analysis to ascertain the functional roles of eL33 in ribosome biogenesis and translation initiation

2022

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An extensive mutational analysis of RPL33A, encoding the yeast ribosomal protein L33A (eL33) allowed us to identify several novel rpl33a mutants with different translational phenotypes. Most of the rpl33a mutants are defective in the processing of 35S and 27S pre-rRNA precursors and the production of mature rRNAs, exhibiting reductions in the amounts of ribosomal subunits and altered polysome profiles. Some of the rpl33a mutants exhibit a Gcd− phenotype of constitutive derepression of GCN4 translation and strong slow growth phenotypes at several temperatures. Interestingly, some of the later mutants also show a detectable increase in the UUG/AUG translation initiation ratio that can be suppressed by eIF1 overexpression, suggesting a requirement for eL33 and a correct 60S/40S subunit ratio for the proper recognition of the AUG start codon. In addition to producing differential reductions in the rates of pre-rRNA maturation and perhaps in r-protein assembly, most of the point rpl33a mutations alter specific molecular interactions of eL33 with the rRNAs and other r-proteins in the 60S structure. Thus, rpl33a mutations cause distinctive effects on the abundance and/or functionality of 60S subunits, leading to more or less pronounced defects in the rates and fidelity of mRNA translation.

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Ribosome cycle—Assembly, degradation, and recycling

Tyagi¹,

Kumar²

2021

Emerging Concepts in Ribosome Structure, Biogenesis, and Function

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Mechanistic insight into eukaryotic 60S ribosomal subunit biogenesis by cryo-electron microscopy

Cited by 58 publications

References 190 publications

A Puzzle of Life: Crafting Ribosomal Subunits

A Puzzle of Life: Crafting Ribosomal Subunits

Wide mutational analysis to ascertain the functional roles of eL33 in ribosome biogenesis and translation initiation

Ribosome cycle—Assembly, degradation, and recycling

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