Final Pre-40S Maturation Depends on the Functional Integrity of the 60S Subunit Ribosomal Protein L3

García-Gómez, Juan José; Fernández-Pévida, Antonio; Lebaron, Simon; Rosado, Iván V.; Tollervey, David; Kressler, Dieter; Cruz, Jesús de la

doi:10.1371/journal.pgen.1004205

Cited by 55 publications

(63 citation statements)

References 71 publications

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“…The uL3 was implicated into eIF5B dependent 3 0 end processing of 18S rRNA in the context of 80S ribosomes that have not yet engaged in translation, underscoring the fact that the GAC and its neighborhood actively participate in the interplay with trGTPases at various steps of ribosomal life. 67 In summary, in this paper, we have clarified the role of the ribosomal protein uL11 showing its modus operandi in the translational apparatus. Using an in vivo approach, we have brought a missing link between structural and biochemical studies, providing the functional picture of the uL11 interplay with trGTPases during translation.…”

Section: Ul11 and Ribosomal Biogenesismentioning

confidence: 86%

Functional analysis of the uL11 protein impact on translational machinery

Wawiórka¹,

Molestak²,

Szajwaj³

et al. 2016

Cell Cycle

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The ribosomal GTPase associated center constitutes the ribosomal area, which is the landing platform for translational GTPases and stimulates their hydrolytic activity. The ribosomal stalk represents a landmark structure in this center, and in eukaryotes is composed of uL11, uL10 and P1/P2 proteins. The modus operandi of the uL11 protein has not been exhaustively studied in vivo neither in prokaryotic nor in eukaryotic cells. Using a yeast model, we have brought functional insight into the translational apparatus deprived of uL11, filling the gap between structural and biochemical studies. We show that the uL11 is an important element in various aspects of 'ribosomal life'. uL11 is involved in 'birth' (biogenesis and initiation), by taking part in Tif6 release and contributing to ribosomal subunit-joining at the initiation step of translation. uL11 is particularly engaged in the 'active life' of the ribosome, in elongation, being responsible for the interplay with eEF1A and fidelity of translation and contributing to a lesser extent to eEF2-dependent translocation. Our results define the uL11 protein as a critical GAC element universally involved in trGTPase 'productive state' stabilization, being primarily a part of the ribosomal element allosterically contributing to the fidelity of the decoding event.

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Section: Ul11 and Ribosomal Biogenesismentioning

confidence: 86%

Functional analysis of the uL11 protein impact on translational machinery

Wawiórka¹,

Molestak²,

Szajwaj³

et al. 2016

Cell Cycle

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“…4B) suggesting rapid processing of this intermediate. In contrast, the yeast 20S pre-rRNA is readily detectable as it is part of the late pre-40S subunit that undergoes tight quality control in the cytoplasm (Lebaron et al 2012;Strunk et al 2012;García-Gómez et al 2014). The 27SA 2 pre-rRNA is further processed in a pathway similar to that used in yeast to generate the short and long forms of the 5.8S rRNA (5.8S S and 5.8S L , respectively) as well as the 25S rRNA (Fig.…”

Section: Discussion Atbrx1 Proteins Are Important For Developmentmentioning

confidence: 99%

atBRX1-1 and atBRX1-2 are involved in an alternative rRNA processing pathway in Arabidopsis thaliana

Weis

Palm

Missbach

et al. 2015

RNA

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Ribosome biogenesis is an essential process in all organisms. In eukaryotes, multiple ribosome biogenesis factors (RBFs) act in the processing of ribosomal (r)RNAs, assembly of ribosomal subunits and their export to the cytoplasm. We characterized two genes in Arabidopsis thaliana coding for orthologs of yeast BRX1, a protein involved in maturation of the large ribosomal subunit. Both atBRX1 proteins, encoded by AT3G15460 and AT1G52930, respectively, are mainly localized in the nucleolus and are ubiquitously expressed throughout plant development and in various tissues. Mutant plant lines for both factors show a delay in development and pointed leaves can be observed in the brx1-2 mutant, implying a link between ribosome biogenesis and plant development. In addition, the pre-rRNA processing is affected in both mutants. Analysis of the pre-rRNA intermediates revealed that early processing steps can occur either in the 5 ′ external transcribed spacer (ETS) or internal transcribed spacer 1 (ITS1). Interestingly, we also find that in xrn2 mutants, early processing events can be bypassed and removal of the 5 ′ ETS is initiated by cleavage at the P ′ processing site. While the pathways of pre-rRNA processing are comparable to those of yeast and mammalian cells, the balance between the two processing pathways is different in plants. Furthermore, plant-specific steps such as an additional processing site in the 5 ′ ETS, likely post-transcriptional processing of the early cleavage sites and accumulation of a 5 ′ extended 5.8S rRNA not observed in other eukaryotes can be detected.

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“…Recruitment of the ATPase Rio1, presumably requiring the prior dissociation of Tsr1 [78], yields late pre-40S ribosomes that are competent to join 60S subunits [79][80][81]. Within these 80S-like ribosomes, Rio1 and the GTPase eIF5B stimulate the Nob1-catalyzed cleavage at site D of the 20S pre-rRNA into mature 18S rRNA [74,80,[82][83][84] (Figures 1 and 2H). Coupling pre-40S maturation to such a quality control step ensures that only properly assembled 40S subunits enter the pool of translating 80S ribosomes.…”

Section: Final Maturation Of Pre-40s Particlesmentioning

confidence: 99%

A Puzzle of Life: Crafting Ribosomal Subunits

Kressler

Hurt

Baßler

2017

Trends in Biochemical Sciences

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165

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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Final Pre-40S Maturation Depends on the Functional Integrity of the 60S Subunit Ribosomal Protein L3

Cited by 55 publications

References 71 publications

Functional analysis of the uL11 protein impact on translational machinery

Functional analysis of the uL11 protein impact on translational machinery

atBRX1-1 and atBRX1-2 are involved in an alternative rRNA processing pathway in Arabidopsis thaliana

A Puzzle of Life: Crafting Ribosomal Subunits

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