ArticleNucleic acids research2004
Identification of a functional core in the RNA component of RNase MRP of budding yeasts.
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 20 papers.
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Who cites it
20 citing papers in PubMed, 34 citations in OpenAlex.
- The Dynamic Network of RNP RNase P Subunits.International journal of molecular sciences · 2021Review
- A Novel Model for the RNase MRP-Induced Switch between the Formation of Different Forms of 5.8S rRNA.International journal of molecular sciences · 2021Article
- Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP.Nature communications · 2020Article
- Comparative genomics of microsporidian genomes reveals a minimal non-coding RNA set and new insights for transcription in minimal eukaryotic genomes.DNA research : an international journal for rapid publication of reports on genes and genomes · 2017Article
- Article
- Structural organizations of yeast RNase P and RNase MRP holoenzymes as revealed by UV-crosslinking studies of RNA-protein interactions.RNA (New York, N.Y.) · 2012Article
- Interactions of a Pop5/Rpp1 heterodimer with the catalytic domain of RNase MRP.RNA (New York, N.Y.) · 2011Article
- Functionally important structural elements of U12 snRNA.Nucleic acids research · 2011Article
- Eukaryotic ribonucleases P/MRP: the crystal structure of the P3 domain.The EMBO journal · 2010Article
- Crystallization and preliminary X-ray diffraction analysis of the P3 RNA domain of yeast ribonuclease MRP in a complex with RNase P/MRP protein components Pop6 and Pop7.Acta crystallographica. Section F, Structural biology and crystallization communications · 2010Article
- RNase MRP is required for entry of 35S precursor rRNA into the canonical processing pathway.RNA (New York, N.Y.) · 2009Article
- Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes.RNA (New York, N.Y.) · 2008Article
- Structural RNAs of known and unknown function identified in malaria parasites by comparative genomics and RNA analysis.RNA (New York, N.Y.) · 2007Article
- Heterodimerization regulates RNase MRP/RNase P association, localization, and expression of Rpp20 and Rpp25.RNA (New York, N.Y.) · 2007Article
- Functional characterization of the conserved amino acids in Pop1p, the largest common protein subunit of yeast RNases P and MRP.RNA (New York, N.Y.) · 2006Article
- Sequence analysis of RNase MRP RNA reveals its origination from eukaryotic RNase P RNA.RNA (New York, N.Y.) · 2006Article
- Current awareness on yeast.Yeast (Chichester, England) · 2005Article
- Identification and analysis of ribonuclease P and MRP RNA in a broad range of eukaryotes.Nucleic acids research · 2005Article
- Article
- Ribonuclease P: the evolution of an ancient RNA enzyme.Critical reviews in biochemistry and molecular biologyArticle
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
RNase MRP is an endonuclease participating in ribosomal RNA processing. It consists of one RNA and at least nine protein subunits. Using oligonucleotide-directed mutagenesis, we analyzed the functional role of five of the hairpins in the secondary structure of the RNA subunit of Saccharomyces cerevisiae RNase MRP. Deletion of an entire hairpin was either lethal or resulted in very poor growth. However, peripheral portions constituting up to 70% of a hairpin could be deleted without effects on cell growth rate or processing of rRNA. To determine whether these hairpins perform redundant functions, we analyzed mutants combining four or five benign hairpin deletions. Simultaneous removal of four of these hairpin segments had no detectable effect. Removing five created a temperature- and cold-sensitive enzyme, but these deficiencies could be partially overcome by a mutation in one of the RNase MRP protein subunits, or by increasing the copy number of several of the protein subunit genes. These observations suggest that the peripheral elements of the RNA hairpins contain no structures or sequences required for substrate recognition, catalysis or binding of protein subunits. Thus, the functionally essential elements of the RNase MRP RNA appear to be concentrated in the core of the subunit.
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Registered trials
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.