ArticleProtein science : a publication of the Protein Society2017
Atomic modeling of the ITS2 ribosome assembly subcomplex from cryo-EM together with mass spectrometry-identified protein-protein crosslinks.
Article in Protein science : a publication of the Protein Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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12 citing papers in PubMed, 20 citations in OpenAlex.
- Structural and functional analysis of a plant nucleolar RNA chaperone-like protein.Scientific reports · 2023Article
- Fast cross-linking by DOPA2 promotes the capturing of a stereospecific protein complex over nonspecific encounter complexes.Biophysics reports · 2022Article
- Sequence-specific remodeling of a topologically complex RNP substrate by Spb4.Nature structural & molecular biology · 2022Article
- The ribosome assembly factor Nop53 has a structural role in the formation of nuclear pre-60S intermediates, affecting late maturation events.Nucleic acids research · 2021Article
- Analyzing Ribosome Remodeling in Health and Disease.Proteomics · 2020Review
- Coupling of 5S RNP rotation with maturation of functional centers during large ribosomal subunit assembly.Nature communications · 2020Article
- The ribosome assembly factor Nop53 controls association of the RNA exosome with pre-60S particles in yeast.The Journal of biological chemistry · 2019Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- The Npa1p complex chaperones the assembly of the earliest eukaryotic large ribosomal subunit precursor.PLoS genetics · 2018Article
- Viewing pre-60S maturation at a minute's timescale.Nucleic acids research · 2018Article
- Predictive and Experimental Approaches for Elucidating Protein-Protein Interactions and Quaternary Structures.International journal of molecular sciences · 2017Review
- Reconstitution of the complete pathway of ITS2 processing at the pre-ribosome.Nature communications · 2017Article
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Authors and funding
5 authors at 4 institutions in 3 countries.
Funding
Abstract
The assembly of ribosomal subunits starts in the nucleus, initiated by co-transcriptional folding of nascent ribosomal RNA (rRNA) transcripts and binding of ribosomal proteins and assembly factors. The internal transcribed spacer 2 (ITS2) is a precursor sequence to be processed from the intermediate 27S rRNA in the nucleoplasm; its removal is required for nuclear export of pre-60S particles. The proper processing of the ITS2 depends on multiple associated assembly factors and RNases. However, none of the structures of the known ITS2-binding factors is available. Here, we describe the modeling of the ITS2 subcomplex, including five assembly factors Cic1, Nop7, Nop15, Nop53, and Rlp7, using a combination of cryo-electron microscopy and cross-linking of proteins coupled with mass spectrometry approaches. The resulting atomic models provide structural insights into their function in ribosome assembly, and establish a framework for further dissection of their molecular roles in ITS2 processing.
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