ArticleNucleic acids research2017
Structural analysis reveals the flexible C-terminus of Nop15 undergoes rearrangement to recognize a pre-ribosomal RNA folding intermediate.
Article in Nucleic acids research, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 10 citations in OpenAlex.
- Intra- and inter-molecular regulation by intrinsically-disordered regions governs PUF protein RNA binding.Nature communications · 2023Article
- The translational repressor Glorund uses interchangeable RNA recognition domains to recognize Drosophila nanos.Nucleic acids research · 2023Article
- Structural and functional analysis of a plant nucleolar RNA chaperone-like protein.Scientific reports · 2023Article
- The Role of ChitooligosaccharidolyticInternational journal of molecular sciences · 2022Article
- Oligomeric transition and dynamics of RNA binding by the HuR RRM1 domain in solution.Journal of biomolecular NMR · 2018Article
- Structural transitions during large ribosomal subunit maturation analyzed by tethered nuclease structure probing in S. cerevisiae.PloS one · 2017Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The RNA recognition motif (RRM) is the most abundant RNA-binding domain in eukaryotes, and it plays versatile roles in RNA metabolism. Despite its abundance, diversity of RRM structure and function is generated by variations on a conserved core. Yeast Nop15 is an RRM protein that is essential for large ribosomal subunit biogenesis. We determined a 2.0 Å crystal structure of Nop15 that reveals a C-terminal α-helical region obscures its canonical RNA-binding surface. Small-angle X-ray scattering, NMR and RNA-binding analyses further reveal that the C-terminal residues of Nop15 are highly flexible, but essential for tight RNA binding. Moreover, comparison with a recently reported cryo-electron microscopy structure indicates that dramatic rearrangement of the C-terminal region of Nop15 in the pre-ribosome exposes the RNA-binding surface to recognize the base of its stem-loop target RNA and extends a newly-formed α helix to the distal loop where it forms protein interactions.
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Registered trials
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