ArticleNucleic acids research2004
Two-hybrid Mpp10p interaction-defective Imp4 proteins are not interaction defective in vivo but do confer specific pre-rRNA processing defects in Saccharomyces cerevisiae.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 21 citations in OpenAlex.
- Genetics animates structure: leveraging genetic interactions to study the dynamics of ribosome biogenesis.Current genetics · 2021Review
- Bud23 promotes the final disassembly of the small subunit Processome in Saccharomyces cerevisiae.PLoS genetics · 2020Article
- Synergistic defects in pre-rRNA processing from mutations in the U3-specific protein Rrp9 and U3 snoRNA.Nucleic acids research · 2020Article
- The Polymorphic PolyQ Tail Protein of the Mediator Complex, Med15, Regulates the Variable Response to Diverse Stresses.International journal of molecular sciences · 2020Article
- Sas10 controls ribosome biogenesis by stabilizing Mpp10 and delivering the Mpp10-Imp3-Imp4 complex to nucleolus.Nucleic acids research · 2019Article
- Crucial role of the Rcl1p-Bms1p interaction for yeast pre-ribosomal RNA processing.Nucleic acids research · 2014Article
- Tissue specific roles for the ribosome biogenesis factor Wdr43 in zebrafish development.PLoS genetics · 2014Article
- Ebp2 and Brx1 function cooperatively in 60S ribosomal subunit assembly in Saccharomyces cerevisiae.Nucleic acids research · 2012Article
- In vivo approaches to dissecting the function of RNA helicases in eukaryotic ribosome assembly.Methods in enzymology · 2012Article
- Assembling a protein-protein interaction map of the SSU processome from existing datasets.PloS one · 2011Article
- A direct interaction between the Utp6 half-a-tetratricopeptide repeat domain and a specific peptide in Utp21 is essential for efficient pre-rRNA processing.Molecular and cellular biology · 2008Article
- Saccharomyces cerevisiae Sof1p associates with 35S Pre-rRNA independent from U3 snoRNA and Rrp5p.Eukaryotic cell · 2006Article
- Deletion of the three distal S1 motifs of Saccharomyces cerevisiae Rrp5p abolishes pre-rRNA processing at site A(2) without reducing the production of functional 40S subunits.Eukaryotic cell · 2004Article
- An overview of pre-ribosomal RNA processing in eukaryotes.Wiley interdisciplinary reviews. RNAReview
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2 authors at 1 institution in 1 country.
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Abstract
The SSU processome is a large, evolutionarily conserved ribonucleoprotein (RNP), consisting of the U3 snoRNA and at least 28 protein components, that is required for biogenesis of the 18S rRNA. We tested the function of one protein-protein interaction in the SSU processome, Mpp10p-Imp4p, in ribosome biogenesis. Exploiting the reverse two-hybrid system, we screened for mutated Imp4 proteins that were conditionally defective for interaction with Mpp10p. Three different imp4 sequences were isolated that: (i) conferred conditional growth in the two-hybrid strain; (ii) complemented the disrupted imp4; (iii) conferred conditional growth in the context of their normal cellular function; and (iv) resulted in defective pre-rRNA processing at the non-permissive temperatures. Domain swapping revealed that mutations that conferred cold sensitivity resided in the N-terminal coiled-coil domain while mutations in the C-terminus conferred temperature sensitivity. Surprisingly, the mutated Imp4 proteins were not measurably defective for interaction with Mpp10p in the context of the SSU processome. This suggests that other members of the complex may contribute to maintaining the Mpp10p-Imp4p interaction in this large RNP. Since protein-protein interactions are critical for many different aspects of cellular metabolism, our work has implications for the study of other large protein complexes.
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