Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors
- Resource Type
- Authors
- Preiss, Thomas; Pöll, Gisela; Pilsl, Michael; Griesenbeck, Joachim; Tschochner, Herbert; Milkereit, Philipp
- Source
- PLoS ONE, Vol 16, Iss 11, p e0252497 (2021)
PLoS ONE
- Subject
- Protein Folding
Molecular biology
Biochemistry
Ribosome
Protein structure
Large ribosomal subunit
RNA Precursors
570 Biowissenschaften, Biologie
Electron Microscopy
RNA structure
Microscopy
Multidisciplinary
Chemistry
Eukaryota
Cell biology
Folding (chemistry)
Nucleic acids
Ribosomal RNA
Ribonucleoproteins
Medicine
ddc:570
Research Article
Ribosomal Proteins
Protein Structure
Cellular structures and organelles
Protein subunit
Science
Protein domain
Saccharomyces cerevisiae
Research and Analysis Methods
Protein–protein interaction
Fungal Proteins
Protein Domains
Ribosomal protein
Non-coding RNA
Biology and life sciences
Organisms
Fungi
Proteins
Electron Cryo-Microscopy
Yeast
Macromolecular structure analysis
RNA
Ribosome Subunits, Large
Ribosomes
- Language
- English
- ISSN
- 1932-6203
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.