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ProteomicsCross-Linking Mass Spectrometry (CXMS) of human pre-60S ribosomal particles
Cross-Linking Mass Spectrometry (CXMS) analysis of human pre-60S ribosomal particles.
ORGANISM(S): Homo Sapiens 
2020-05-07 | PXD019025 |
ProteomicsEffect of Nop53 depletion on the compositional changes during pre-60S maturation
The eukaryotic ribosome biogenesis is a highly orchestrated multistep process that starts at the nucleolus with the transcription of pre-rRNAs 5S and 35S. The latter comprises the mature 18S, 5.8S and 25S rRNAs separated by internal transcribed spacers (ITS1 and ITS2) and externally flanked by the 5...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2021-09-09 | PXD023383 | Pride
Nop53 Eukaryotic ribosome biogenesis Pre-60s S. cerevisiae 
ProteomicsRbp95 binds 25S rRNA helix H95 and cooperates with the Npa1 complex during early pre-60S particle maturation
Eukaryotic ribosome synthesis involves more than 200 assembly factors, which promote ribosomal RNA (rRNA) processing, modification and folding, and assembly of ribosomal proteins. The formation and maturation of the earliest pre-60S particles requires structural remodeling by the Npa1 complex, but i...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2022-10-13 | PXD030106 | Pride
Ribosome assembly factor Yeast S. cerevisiae Tandem-affinity purification (tap) Npa1 Pre-60s particles Rbp95 
ProteomicsDiverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomal particles
Ribosome biogenesis is a highly complex process in eukaryotes, involving temporally and spatially regulated ribosomal protein (r-protein) binding and rRNA remodeling events in the nucleolus, nucleoplasm and cytoplasm. Hundreds of assembly factors (AFs), organized into sequential functional groups, f...
ORGANISM(S): Saccharomyces cerevisiae (Baker's yeast) 
2016-06-01 | PXD003736 | Pride
Assembly factors Cryo-em Pre-60s ribosome Cxms 
ProteomicsIdentification of 60S pre-rRNA binding sites of human GNL3L GTPase
We reveal that the GNL3 paralogue GTPase, GNL3L, associates with pre-ribosomes. We map RNA contact sites on GNL3L as well as GNL3L binding sites on pre-rRNAs. Lack of GNL3L impairs synthesis of the 60S rRNAs and expression of GTPase inactive GNL3L causes defects in early steps of pre-rRNA processing...
ORGANISM(S): Homo sapiens (Human) 
2026-03-05 | PXD067606 | Pride
Human Gtpase Gnl3l 60s rrna Rna-protein crosslinking 
ProteomicsDistinct steps of nuclear maturation of human pre-60S complexes require the activity of GTPases, including GNL3L
Production of the eukaryotic ribosomal subunits (40S and 60S) is a highly dynamic process in which numerous assembly factors coordinate structural rearrangements of pre-ribosomal complexes to achieve their mature, functional architectures. Across the domains of life, GTPases leverage their functions...
ORGANISM(S): Homo sapiens (Human) 
2026-03-09 | PXD068314 | Pride
Ribosome biogenesis Gtpase Ribosomal protein Gtpbp4 Gnl2 Pre-rrna processing Gnl3 Translation 
ProteomicsNascent alt-protein chemoproteomics reveals a repressor of ribosome biogenesisNascent alt-protein chemoproteomics reveals a repressor of pre-60S assembly
Many unannotated microproteins and alternative proteins (alt-proteins) have recently been found to be co-encoded with canonical proteins, but few of their functions are known. Motivated by the hypothesis that alt-proteins undergoing regulated synthesis could play important cellular roles, we develop...
ORGANISM(S): Homo sapiens (Human) 
2022-09-13 | PXD026880 | Pride
Human hek 293t Lc-ms/ms 
UnknownEmergence of the primordial pre-60S from the 90S pre-ribosome.
Not available
S-EPMC8994135 | biostudies-literature
ProteomicsNuclear VCP-like 2 (NVL2)-associated complex
LC-MSMS analysis of NVL2-associated pre-60S complex. To obtain more insights into the molecular mechanism of this effects caused by the mutant NVL2 in pre-60S complexes,we searched for additional proteins that preferentially interact with the NVL2(E365Q/E682Q) in comparison with wild-type NVL2. Co-m...
ORGANISM(S): Homo Sapiens (human) 
2025-01-31 | PXD057741 | JPOST Repository
UnknownMak5 and Ebp2 act together on early pre-60S particles and their reduced functionality bypasses the requirement for the essential pre-60S factor Nsa1.
Not available
S-EPMC3846774 | biostudies-literature
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