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TitleA comprehensive view on r-protein binding and rRNA domain structuring during early eukaryotic ribosome formation.
Journal, issue, pagesNucleic Acids Res, Vol. 54, Issue 3, Year 2026
Publish dateJan 22, 2026
AuthorsMagdalena Gerhalter / Michael Prattes / Lorenz Emanuel Grundmann / Irina Grishkovskaya / Enrico F Semeraro / Gertrude Zisser / Harald Kotisch / Juliane Merl-Pham / Stefanie M Hauck / David Haselbach / Helmut Bergler /
PubMed AbstractFormation of the eukaryotic ribosomal subunits follows a strict regime to assemble ribosomal proteins (r-protein) with ribosomal RNAs (rRNA) while removing internal (ITS) and external (ETS) ...Formation of the eukaryotic ribosomal subunits follows a strict regime to assemble ribosomal proteins (r-protein) with ribosomal RNAs (rRNA) while removing internal (ITS) and external (ETS) transcribed rRNA spacers. During the early stages of large subunit (LSU) formation, ITS2, together with six assembly factors, forms the characteristic foot structure of early nuclear pre-LSU particles. Here, we address the function of this foot structure during the early stages of ribosome assembly. We present cryo-EM structures from wild-type cells and cells depleted for the foot structure factor Rlp7. We show that compaction of domain I of the 25S rRNA is strictly dependent on the presence of foot factors, while domain II folds independently. Furthermore, Rlp7-depletion accumulated small subunit (SSU) processome intermediates prior to A1 cleavage and compaction of the individual domains of the 18S rRNA, providing also novel insights into the SSU-assembly process. SILAC labeling and affinity purification of co-transcriptionally assembled pre-ribosomes enabled us to resolve the assembly line of most early binding r-proteins step by step. This showed that incorporation of r-proteins in eukaryotes neither follows the bacterial regime nor a strict linear co-transcriptional mode. Instead, seed r-proteins might structurally define the individual rRNA domains before their compaction and fixation in the context of early pre-ribosomes.
External linksNucleic Acids Res / PubMed:41569156 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.4 Å
Structure data

53201

9qjc

EMDB-53201, PDB-9qjc:
Yeast pre-60S Domain II intermediate
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-55356: Noc2-TAP pre-60S particle - state 1
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-55368: Noc2-TAP pre-60S particle - state 2
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-55840: Noc2-TAP pre-60S particle - state 3
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-55843: Noc2-TAP 90S particle - state A1
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-55860: Noc2-TAP 90S particle - state A2
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-55874: Noc2-TAP 90S particle - state A3
Method: EM (single particle) / Resolution: 3.4 Å

Source
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsRIBOSOME / preLSU / preribosome / complex / Noc2-TAP particle

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