ArticleMolecular and cellular biology2006
Protein-protein and protein-RNA contacts both contribute to the 15.5K-mediated assembly of the U4/U6 snRNP and the box C/D snoRNPs.
Article in Molecular and cellular biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
29 citing papers in PubMed, 47 citations in OpenAlex.
- RNA-binding proteins that lack canonical RNA-binding domains are rarely sequence-specific.Scientific reports · 2023Article
- Eukaryotic Box C/D methylation machinery has two non-symmetric protein assembly sites.Scientific reports · 2021Article
- Disruption of exon-bridging interactions between the minor and major spliceosomes results in alternative splicing around minor introns.Nucleic acids research · 2021Article
- NOPCHAP1 is a PAQosome cofactor that helps loading NOP58 on RUVBL1/2 during box C/D snoRNP biogenesis.Nucleic acids research · 2021Article
- A conserved Bcd1 interaction essential for box C/D snoRNP biogenesis.The Journal of biological chemistry · 2019Article
- The multistructural forms of box C/D ribonucleoprotein particles.RNA (New York, N.Y.) · 2018Review
- The host-encoded RNase E endonuclease as the crRNA maturation enzyme in a CRISPR-Cas subtype III-Bv system.Nature microbiology · 2018Article
- Sequence determinants of the folding properties of box C/D kink-turns in RNA.RNA (New York, N.Y.) · 2017Article
- Control of box C/D snoRNP assembly by NEMBO reports · 2017Article
- Implication of the box C/D snoRNP assembly factor Rsa1p in U3 snoRNP assembly.Nucleic acids research · 2017Article
- Assembly and trafficking of box C/D and H/ACA snoRNPs.RNA biology · 2017Review
- Epigenome-wide association study of smoking and DNA methylation in non-small cell lung neoplasms.Oncotarget · 2016Article
- SIRT7-dependent deacetylation of the U3-55k protein controls pre-rRNA processing.Nature communications · 2016Article
- Proteomic and 3D structure analyses highlight the C/D box snoRNP assembly mechanism and its control.The Journal of cell biology · 2014Article
- Biochemical defects in minor spliceosome function in the developmental disorder MOPD I.RNA (New York, N.Y.) · 2014Article
- Characterization of the interaction between protein Snu13p/15.5K and the Rsa1p/NUFIP factor and demonstration of its functional importance for snoRNP assembly.Nucleic acids research · 2014Article
- Post-transcriptional regulation of myotube elongation and myogenesis by Hoi Polloi.Development (Cambridge, England) · 2013Article
- Structural and functional analysis of the U3 snoRNA binding protein Rrp9.RNA (New York, N.Y.) · 2013Article
- PHF6 regulates cell cycle progression by suppressing ribosomal RNA synthesis.The Journal of biological chemistry · 2013Article
- A novel Nop5-sRNA interaction that is required for efficient archaeal box C/D sRNP formation.RNA (New York, N.Y.) · 2010Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The k-turn-binding protein 15.5K is unique in that it is essential for the hierarchical assembly of three RNP complexes distinct in both composition and function, namely, the U4/U6 snRNP, the box C/D snoRNP, and the RNP complex assembled on the U3 box B/C motif. 15.5K interacts with the cognate RNAs via an induced fit mechanism, which results in the folding of the surrounding RNA to create a binding site(s) for the RNP-specific proteins. However, it is possible that 15.5K also mediates RNP formation via protein-protein interactions with the complex-specific proteins. To investigate this possibility, we created a series of 15.5K mutations in which the surface properties of the protein had been changed. We assessed their ability to support the formation of the three distinct RNP complexes and found that the formation of each RNP requires a distinct set of regions on the surface of 15.5K. This implies that protein-protein contacts are essential for RNP formation in each complex. Further supporting this idea, direct protein-protein interaction could be observed between hU3-55K and 15.5K. In conclusion, our data suggest that the formation of each RNP involves the direct recognition of specific elements in both 15.5K protein and the specific RNA.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.