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8C01

Enp1TAP_A population of yeast small ribosomal subunit precursors

Summary for 8C01
Entry DOI10.2210/pdb8c01/pdb
EMDB information16348 16349 16360 16361
Descriptor18S rRNA precursor, 40S ribosomal protein S0-A, 40S ribosomal protein S1-A, ... (32 entities in total)
Functional Keywordsribosomal assembly state, ribosome
Biological sourceSaccharomyces cerevisiae (baker's yeast)
More
Total number of polymer chains31
Total formula weight1312965.46
Authors
Milkereit, P.,Poell, G. (deposition date: 2022-12-15, release date: 2022-12-28, Last modification date: 2024-07-24)
Primary citationPoll, G.,Griesenbeck, J.,Tschochner, H.,Milkereit, P.
Impact of the yeast S0/uS2-cluster ribosomal protein rpS21/eS21 on rRNA folding and the architecture of small ribosomal subunit precursors.
Plos One, 18:e0283698-e0283698, 2023
Cited by
PubMed Abstract: RpS0/uS2, rpS2/uS5, and rpS21/eS21 form a cluster of ribosomal proteins (S0-cluster) at the head-body junction near the central pseudoknot of eukaryotic small ribosomal subunits (SSU). Previous work in yeast indicated that S0-cluster assembly is required for the stabilisation and maturation of SSU precursors at specific post-nucleolar stages. Here, we analysed the role of S0-cluster formation for rRNA folding. Structures of SSU precursors isolated from yeast S0-cluster expression mutants or control strains were analysed by cryogenic electron microscopy. The obtained resolution was sufficient to detect individual 2'-O-methyl RNA modifications using an unbiased scoring approach. The data show how S0-cluster formation enables the initial recruitment of the pre-rRNA processing factor Nob1 in yeast. Furthermore, they reveal hierarchical effects on the pre-rRNA folding pathway, including the final maturation of the central pseudoknot. Based on these structural insights we discuss how formation of the S0-cluster determines at this early cytoplasmic assembly checkpoint if SSU precursors further mature or are degraded.
PubMed: 36996028
DOI: 10.1371/journal.pone.0283698
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.7 Å)
Structure validation

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