Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors.
Journal
PloS one
ISSN: 1932-6203
Titre abrégé: PLoS One
Pays: United States
ID NLM: 101285081
Informations de publication
Date de publication:
2021
2021
Historique:
received:
14
05
2021
accepted:
17
10
2021
entrez:
23
11
2021
pubmed:
24
11
2021
medline:
30
12
2021
Statut:
epublish
Résumé
In yeast and human cells many of the ribosomal proteins (r-proteins) are required for the stabilisation and productive processing of rRNA precursors. Functional coupling of r-protein assembly with the stabilisation and maturation of subunit precursors potentially promotes the production of ribosomes with defined composition. To further decipher mechanisms of such an intrinsic quality control pathway we analysed here the contribution of three yeast large ribosomal subunit r-proteins rpL2 (uL2), rpL25 (uL23) and rpL34 (eL34) for intermediate nuclear subunit folding steps. Structure models obtained from single particle cryo-electron microscopy analyses provided evidence for specific and hierarchic effects on the stable positioning and remodelling of large ribosomal subunit domains. Based on these structural and previous biochemical data we discuss possible mechanisms of r-protein dependent hierarchic domain arrangement and the resulting impact on the stability of misassembled subunits.
Identifiants
pubmed: 34813592
doi: 10.1371/journal.pone.0252497
pii: PONE-D-21-15939
pmc: PMC8610266
doi:
Substances chimiques
Fungal Proteins
0
RNA Precursors
0
Ribosomal Proteins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
e0252497Subventions
Organisme : NIGMS NIH HHS
ID : R01 GM129325
Pays : United States
Déclaration de conflit d'intérêts
The authors have declared that no competing interests exist.
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