Rbp95 binds to 25S rRNA helix H95 and cooperates with the Npa1 complex during early pre-60S particle maturation

Bhutada, Priya; Favre, Sébastien; Jaafar, Mariam; Hafner, Jutta; Liesinger, Laura; Unterweger, Stefan; Bischof, Karin; Darnhofer, Barbara; Sankar, Devanarayanan Siva; Rechberger, Gerald; Merhi, Raghida Abou; Lebaron, Simon; Birner‐Gruenberger, Ruth; Kressler, Dieter; Henras, Anthony K.; Pertschy, Brigitte

doi:10.1093/nar/gkac724

Cited by 5 publications

(2 citation statements)

References 76 publications

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“…Thus, it is possible that separation of the nascent 40S and 60S molecules requires not just the Rrp5/Rcl1-regulated cleavage step but additional 60S maturation steps. Intriguingly, additional data link early rRNA modification events in domain V to this separation step ( Bhutada et al, 2022 ; Ismail et al, 2022 ; Aquino et al, 2021 ; Joret et al, 2018 ), although the details, as well as the possibility that this involves a QC checkpoint for rRNA modification or folding remain to be investigated.…”

Section: Ribosome Assembly At a Glancementioning

confidence: 99%

Quality control ensures fidelity in ribosome assembly and cellular health

Parker

Karbstein

2023

Journal of Cell Biology

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The coordinated integration of ribosomal RNA and protein into two functional ribosomal subunits is safeguarded by quality control checkpoints that ensure ribosomes are correctly assembled and functional before they engage in translation. Quality control is critical in maintaining the integrity of ribosomes and necessary to support healthy cell growth and prevent diseases associated with mistakes in ribosome assembly. Its importance is demonstrated by the finding that bypassing quality control leads to misassembled, malfunctioning ribosomes with altered translation fidelity, which change gene expression and disrupt protein homeostasis. In this review, we outline our understanding of quality control within ribosome synthesis and how failure to enforce quality control contributes to human disease. We first provide a definition of quality control to guide our investigation, briefly present the main assembly steps, and then examine stages of assembly that test ribosome function, establish a pass–fail system to evaluate these functions, and contribute to altered ribosome performance when bypassed, and are thus considered “quality control.”

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Section: Ribosome Assembly At a Glancementioning

confidence: 99%

Quality control ensures fidelity in ribosome assembly and cellular health

Parker

Karbstein

2023

Journal of Cell Biology

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“…The following supporting information can be downloaded at https:// www.mdpi.com/article/10.3390/biom13071127/s1: Figure S1: Sequence and structure [44] of Rps2; Figure S2: Localization of Rps2(76-145).R95R97K99>A-3xyEGFP; Figure S3: Nuclear import of Rps2(76-145)-3xyEGFP; Figure S4: TurboID-based proximity labeling using Rps2, Rps2(1-145), and Rps2(76-145), all with and without the R95R97K99>A exchanges, as baits; Figure S5 S1: Yeast strains [7,15,18,23,[45][46][47][48][49]; Table S2: S. cerevisiae plasmids [7,16,43,50,51]; Table S3: TurboID proximity labeling data. S3.…”

Section: Supplementary Materialsmentioning

confidence: 99%

Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5)

Steiner,

Favre,

Mack

et al. 2023

Biomolecules

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The ribosome is assembled in a complex process mainly taking place in the nucleus. Consequently, newly synthesized ribosomal proteins have to travel from the cytoplasm into the nucleus, where they are incorporated into nascent ribosomal subunits. In this study, we set out to investigate the mechanism mediating nuclear import of the small subunit ribosomal protein Rps2. We demonstrate that an internal region in Rps2, ranging from amino acids 76 to 145, is sufficient to target a 3xyEGFP reporter to the nucleus. The importin-β Pse1 interacts with this Rps2 region and is involved in its import, with Rps2 residues arginine 95, arginine 97, and lysine 99 being important determinants for both Pse1 binding and nuclear localization. Moreover, our data reveal a second import mechanism involving the N-terminal region of Rps2, which depends on the presence of basic residues within amino acids 10 to 28. This Rps2 segment overlaps with the binding site of the dedicated chaperone Tsr4; however, the nuclear import of Rps2 via the internal as well as the N-terminal nuclear-targeting element does not depend on Tsr4. Taken together, our study has unveiled hitherto undescribed nuclear import signals, showcasing the versatility of the mechanisms coordinating the nuclear import of ribosomal proteins.

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The snoRNP chaperone snR190 and the Npa1 complex form a macromomecular assembly required for 60S ribosomal subunit maturation

Hamze,

Jaafar,

Khreiss

et al. 2024

Preprint

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The early steps of large-ribosomal-subunit assembly feature among the least understood steps of ribosome synthesis in eukaryotes. In Saccharomyces cerevisiae, the snR190 box C/D snoRNP chaperone and the Npa1 complex, composed of the α-solenoid scaffold proteins Npa1 and Npa2, the DEAD-box helicase Dbp6, the RNA-binding protein Nop8 and Rsa3, are likely involved in early 25S rRNA folding events. Here, we report for the first time the existence outside pre-ribosomal particles of an independent macromolecular assembly constituted by the Npa1 complex and the snR190 snoRNP chaperone. Nop8 mediates the formation of this assembly and can associate on its own with free snR190. Moreover, Nop8 RRM domain helps tether the snR190 snoRNP to pre-ribosomal particles. snR190 features a specific central stem-loop structure, which is required for high-affinity binding between free snR190 and the Npa1 complex. Deleting this extension does not prevent snR190 association with pre-ribosomal particles but impairs snR190 activity in early pre-rRNA processing events. This work establishes the importance of association with auxiliary protein complexes for optimum snoRNP chaperone activity during rRNA folding events.

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Rbp95 binds to 25S rRNA helix H95 and cooperates with the Npa1 complex during early pre-60S particle maturation

Cited by 5 publications

References 76 publications

Quality control ensures fidelity in ribosome assembly and cellular health

Quality control ensures fidelity in ribosome assembly and cellular health

Dissecting the Nuclear Import of the Ribosomal Protein Rps2 (uS5)

The snoRNP chaperone snR190 and the Npa1 complex form a macromomecular assembly required for 60S ribosomal subunit maturation

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