ArticleRNA (New York, N.Y.)2011
The roles of S1 RNA-binding domains in Rrp5's interactions with pre-rRNA.
Article in RNA (New York, N.Y.), 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 27 citations in OpenAlex.
- Trehalase Inhibitor Validamycin May Have Additional Mechanisms of Toxicology againstJournal of fungi (Basel, Switzerland) · 2023Article
- Quality control ensures fidelity in ribosome assembly and cellular health.The Journal of cell biology · 2023Review
- PNPase and RhlB Interact and Reduce the Cellular Availability of Oxidized RNA inMicrobiology spectrum · 2022Article
- The DEAD-Box Protein Rok1 Coordinates Ribosomal RNA Processing in Association with Rrp5 inInternational journal of molecular sciences · 2022Article
- Genome-wide association studies reveal putative QTLs for physiological traits under contrasting phosphorous conditions in wheat (Frontiers in genetics · 2022Article
- The RNA helicase Dbp7 promotes domain V/VI compaction and stabilization of inter-domain interactions during early 60S assembly.Nature communications · 2021Article
- Protein Footprinting via Covalent Protein Painting Reveals Structural Changes of the Proteome in Alzheimer's Disease.Journal of proteome research · 2021Article
- Roles of Organellar RNA-Binding Proteins in Plant Growth, Development, and Abiotic Stress Responses.International journal of molecular sciences · 2020Review
- Rrp5 establishes a checkpoint for 60S assembly during 40S maturation.RNA (New York, N.Y.) · 2019Article
- Ribosome assembly coming into focus.Nature reviews. Molecular cell biology · 2019Review
- Cold Acclimation Improves the Desiccation Stress Resilience of Polar Strains ofFrontiers in microbiology · 2019Article
- Structural and interaction analysis of the Rrp5 C-terminal region.FEBS open bio · 2018Article
- The DEAD-box Protein Rok1 Orchestrates 40S and 60S Ribosome Assembly by Promoting the Release of Rrp5 from Pre-40S Ribosomes to Allow for 60S Maturation.PLoS biology · 2016Article
- Rrp5 binding at multiple sites coordinates pre-rRNA processing and assembly.Molecular cell · 2013Article
- Identification of the binding site of Rlp7 on assembling 60S ribosomal subunits in Saccharomyces cerevisiae.RNA (New York, N.Y.) · 2013Article
- Has1 regulates consecutive maturation and processing steps for assembly of 60S ribosomal subunits.Nucleic acids research · 2013Article
- Cofactor-dependent specificity of a DEAD-box protein.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- 40S ribosome biogenesis co-factors are essential for gametophyte and embryo development.PloS one · 2013Article
- Rrp5p, Noc1p and Noc2p form a protein module which is part of early large ribosomal subunit precursors in S. cerevisiae.Nucleic acids research · 2013Article
- Inside the 40S ribosome assembly machinery.Current opinion in chemical biology · 2011Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
RNA-binding proteins mediate the function of all RNAs. Since few distinct RNA-binding domains (RBDs) exist, with most RBDs contacting only a few nucleotides, RNA-binding proteins often combine multiple RNA-binding motifs to achieve a higher affinity and selectivity for their targets. Rrp5, a ribosome assembly factor essential for both 40S and 60S ribosome maturation, is an extreme example as it contains 12 tandem S1 RNA-binding domains. In this study, we use a combination of RNA binding and DMS probing experiments to probe interactions of Rrp5 with pre-rRNA mimics. Our data localize Rrp5's binding site to three distinct regions within internal transcribed spacer 1 (ITS1), the sequence between 18S and 5.8S rRNAs. One of these regions is directly adjacent to a recently uncovered helical structure, which prevents premature cleavage at the 3'-end of 18S rRNA. This finding, together with previous results, suggests a role for Rrp5 in regulating the above-mentioned helical element. Furthermore, we have produced two truncated forms of the protein, Rrp5N and Rrp5C, which together encompass the entire protein and fully restore growth. Quantitative analysis of the RNA affinity of these Rrp5 fragments indicates that the first nine S1 motifs contribute much of Rrp5's RNA affinity, while the last three domains alone provide its specificity for the pre-rRNA. This surprising division of labor is unique, as it suggests that S1 domains can bind RNA both specifically as well as nonspecifically with high affinity; this has important implications for the molecular details of the Rrp5•pre-rRNA complex.
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