ArticleScientific reports2019
Yeast R2TP Interacts with Extended Termini of Client Protein Nop58p.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 7 citations in OpenAlex.
- Co-translational determination of quaternary structures in chaperone factories.Nature communications · 2026Article
- Differential roles of putative arginine fingers of AAAbioRxiv : the preprint server for biology · 2024Article
- Maturation of small nucleolar RNAs: from production to function.RNA biology · 2023Review
- Artificial intelligence-assisted cryoEM structure of Bfr2-Lcp5 complex observed in the yeast small subunit processome.Communications biology · 2022Article
- The Mammalian Ecdysoneless Protein Interacts with RNA Helicase DDX39A To Regulate Nuclear mRNA Export.Molecular and cellular biology · 2021Article
- High-resolution structure of eukaryotic Fibrillarin interacting with Nop56 amino-terminal domain.RNA (New York, N.Y.) · 2021Article
- NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis.Nucleic acids research · 2021Article
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Authors and funding
11 authors at 1 institution in 1 country.
Funding
Abstract
The AAA + ATPase R2TP complex facilitates assembly of a number of ribonucleoprotein particles (RNPs). Although the architecture of R2TP is known, its molecular basis for acting upon multiple RNPs remains unknown. In yeast, the core subunit of the box C/D small nucleolar RNPs, Nop58p, is the target for R2TP function. In the recently observed U3 box C/D snoRNP as part of the 90 S small subunit processome, the unfolded regions of Nop58p are observed to form extensive interactions, suggesting a possible role of R2TP in stabilizing the unfolded region of Nop58p prior to its assembly. Here, we analyze the interaction between R2TP and a Maltose Binding Protein (MBP)-fused Nop58p by biophysical and yeast genetics methods. We present evidence that R2TP interacts largely with the unfolded termini of Nop58p. Our results suggest a general mechanism for R2TP to impart specificity by recognizing unfolded regions in its clients.
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