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Suppressed 60S ribosome exportation in maize ribosome export associated 1 mutant triggers inconsistent transcriptional and translational regulations

ABSTRACT: Suppressed 60S ribosome exportation in maize ribosome export associated 1 mutant triggers inconsistent transcriptional and translational regulations

PROVIDER: PRJNA278959 | ENA |

REPOSITORIES: ENA

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Suppressed 60S ribosome exportation in maize ribosome export associated 1 mutant triggers inconsistent transcriptional and translational regulations

Project description:This SuperSeries is composed of the SubSeries listed below. Refer to individual Series

2015-04-25 | E-GEOD-67103 | biostudies-arrayexpress

Suppressed 60S ribosome exportation in maize ribosome export associated 1 mutant triggers inconsistent transcriptional and translational regulations

Project description:This SuperSeries is composed of the SubSeries listed below.

2015-04-25 | GSE67103 | GEO

A comprehensive landscape of 60S ribosome biogenesis factors

Project description:We used quantitative proteomics and crosslinking mass spectrometry (XL-MS) to analyse a comprehensive set of purified pre-60S ribosomal particles, obtaining a detailed timeline of RBF engagement during 60S ribosome biogenesis as well as particle-specific crosslink networks for all analysed particles. Our data provide an important resource for all future structural and biochemical studies of 60S ribosome biogenesis.

2021-12-07 | PXD021831 | Pride

Hcr1/eIF3j is a 60S ribosomal subunit recycling accessory factor in vivo

Project description:Hcr1/eIF3j is a sub-stoichiometric subunit of eukaryotic initiation factor 3 (eIF3) that can dissociate the post-termination 40S ribosomal subunit from mRNA in vitro. We examined this ribosome recycling role in vivo by ribosome profiling and reporter assays and found that loss of Hcr1 led to reinitiation of translation in 3’UTRs, consistent with a defect in recycling. However, the defect appeared to be in recycling of the 60S subunit, rather than the 40S subunit, because reinitiation did not require an AUG codon and was suppressed by overexpression of the 60S dissociation factor Rli1/ABCE1. Consistent with a 60S recycling role, overexpression of Hcr1 could not compensate for loss of 40S recycling factors Tma64/eIF2D and Tma20/MCT-1. Intriguingly, loss of Hcr1 triggered higher expression of RLI1 via an apparent feedback loop. These findings suggest Hcr1/eIF3j is recruited to ribosomes at stop codons and may coordinate the transition to a new round of translation.

2019-05-23 | GSE124204 | GEO

Puf6 primes nuclear export of 60S pre-ribosomes at low temperature

Project description:Puf6 primes nuclear export of 60S pre-ribosomes at low temperature

| PRJNA730580 | ENA

High-throughput RNA structure probing reveals critical folding events during early 60S ribosome assembly in yeast.

Project description:While the protein composition of various yeast 60S ribosomal subunit assembly intermediates has been studied in detail, little is known about ribosomal RNA (rRNA) structural rearrangements that take place during early 60S assembly steps. Using a high-throughput RNA structure probing method, we provide nucleotide resolution insights into rRNA structural rearrangements during nucleolar 60S assembly. Our results suggest that many rRNA-folding steps, such as folding of 5.8S rRNA, occur at a very specific stage of assembly, and propose that downstream nuclear assembly events can only continue once 5.8S folding has been completed. Our maps of nucleotide flexibility enable making predictions about the establishment of protein-rRNA interactions, providing intriguing insights into the temporal order of protein-rRNA as well as long-range inter-domain rRNA interactions. These data argue that many distant domains in the rRNA can assemble simultaneously during early 60S assembly and underscore the enormous complexity of 60S synthesis.Ribosome biogenesis is a dynamic process that involves the ordered assembly of ribosomal proteins and numerous RNA structural rearrangements. Here the authors apply ChemModSeq, a high-throughput RNA structure probing method, to quantitatively measure changes in RNA flexibility during the nucleolar stages of 60S assembly in yeast.

2017-10-04 | GSE83821 | GEO

Structure of the AAA-ATPase Drg1 during extraction of Rlp24 from pre-60S particles

Project description:The AAA-ATPase Drg1 is a key factor in eukaryotic ribosome biogenesis that initiates cytoplasmic maturation of the large ribosomal subunit. Drg1 releases the shuttling maturation factor Rlp24 from pre-60S particles shortly after nuclear export, a strict requirement for downstream maturation. The molecular mechanism of release remained elusive. Here, we report a series of cryo-EM structures showing a hand-over-hand translocation mechanism of Drg1 and additional XL-MS data on positioning of Drg1 on pre-60S particles.

2022-10-14 | PXD032098 | Pride

Puf6 primes 60S pre-ribosome nuclear export at low temperature.

Project description: Not available

| S-EPMC8338941 | biostudies-literature

The translation release factor methyltransferase Mtq2-Trm112 is required for ribosome biogenesis

Project description:The Mtq2-Trm112 methyltransferase is known to modify the translational eukaryotic release factor eRF1 on the glutamine side chain of a universally conserved GGQ motif, which is essential to translation termination. The exact role of eRF1 methylation remains unknown. As the deletion of MTQ2 leads to severe growth impairment in S. cerevisiae, we have investigated its role further. Here we report an unexpected function of Mtq2 in ribosome biogenesis. We reveal that Mtq2 is part of nuclear precursor ribosomes to 60S subunits, and we demonstrate that its catalytic activity is required for the stable production of mature 5.8S and 25S rRNAs and for pre-60S export. Consistently, in the absence of Mtq2 function pre-60S subunits enriched in the export factors Nmd3 and Arx1 accumulate in the nucleus. We conclude that, in addition to its role as a translation terminator modification enzyme, Mtq2 is a ribosome assembly factor which is important for late-stage large ribosomal subunit formation.

2020-10-12 | PXD018733 | Pride

The E3 SUMO ligase Mms21 controls ribosome biogenesis

Project description:The budding yeast E3 SUMO ligase Mms21, a component of the Smc5-6 complex, regulates sister chromatid cohesion, DNA replication, and DNA repair. We identify a role for Mms21 in ribosome biogenesis. The mms21RINGD mutant exhibits reduced rRNA production, nuclear accumulation of 60S and 40S ribosomal proteins, and elevated Gcn4 translation. Genes involved in ribosome biogenesis and translation are down-regulated in the mms21RINGD mutant. Examining gene expression profile of mms21RINGD mutant compared to wild-type by RNA Seq using Ilumina sequencing

2015-06-13 | E-GEOD-69826 | biostudies-arrayexpress

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