7OHU

Nog1-TAP associated immature ribosomal particles from S. cerevisiae after rpL2 expression shut down, population B

This is a non-PDB format compatible entry.

Summary for 7OHU

• Entry DOI: 10.2210/pdb7ohu/pdb
• EMDB information: 12909
• Descriptor: 25S rRNA, 60S ribosomal protein L14-A, 60S ribosomal protein L15-A, ... (28 entities in total)
• Functional Keywords: ribosomal assembly state, ribosome
• Biological source: Saccharomyces cerevisiae S288C; More
• Total number of polymer chains: 27
• Total formula weight: 1747629.57

Authors

Milkereit, P.,Poell, G. (deposition date: 2021-05-11, release date: 2021-11-03, Last modification date: 2024-07-10)

Primary citation

Poll, G.,Pilsl, M.,Griesenbeck, J.,Tschochner, H.,Milkereit, P.
Analysis of subunit folding contribution of three yeast large ribosomal subunit proteins required for stabilisation and processing of intermediate nuclear rRNA precursors.
Plos One, 16:e0252497-e0252497, 2021

PubMed Abstract: 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.

PubMed: 34813592
DOI: 10.1371/journal.pone.0252497

Experimental method

ELECTRON MICROSCOPY (3.7 Å)