ArticleRNA (New York, N.Y.)2006
Differential association of protein subunits with the human RNase MRP and RNase P complexes.
Article in RNA (New York, N.Y.), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 59 citations in OpenAlex.
- Identification of RMP24 and RMP64, human ribonuclease MRP-specific protein components.Cell reports · 2025Article
- Reversible proliferative arrest induced by rapid depletion of RNase MRP.Nature communications · 2025Article
- DCAF13-mediated K63-linked ubiquitination of RNA polymerase I promotes uncontrolled proliferation in Breast Cancer.Nature communications · 2025Article
- Evolution of sequence, structural and functional diversity of the ubiquitous DNA/RNA-binding Alba domain.Scientific reports · 2024Article
- RNase P: Beyond Precursor tRNA Processing.Genomics, proteomics & bioinformatics · 2024Review
- Coevolution of RNA and protein subunits in RNase P and RNase MRP, two RNA processing enzymes.The Journal of biological chemistry · 2024Review
- A Novel Method to Isolate RNase MRP Using RNA Streptavidin Aptamer Tags.Bio-protocol · 2023Article
- A novel experimental approach for the selective isolation and characterization of human RNase MRP.RNA biology · 2022Article
- New insights into the role of ribonuclease P protein subunit p30 from tumor to internal reference.Frontiers in oncology · 2022Review
- Deregulated molecules and pathways in the predisposition and dissemination of breast cancer cells to bone.Computational and structural biotechnology journal · 2022Article
- The Short- and Long-Range RNA-RNA Interactome of SARS-CoV-2.Molecular cell · 2020Article
- Crystal Structure of Human Rpp20/Rpp25 Reveals Quaternary Level Adaptation of the Alba Scaffold as Structural Basis for Single-stranded RNA Binding.Journal of molecular biology · 2018Article
- Expression of RMRP RNA is regulated in chondrocyte hypertrophy and determines chondrogenic differentiation.Scientific reports · 2017Article
- A role of human RNase P subunits, Rpp29 and Rpp21, in homology directed-repair of double-strand breaks.Scientific reports · 2017Article
- Targeted CRISPR disruption reveals a role for RNase MRP RNA in human preribosomal RNA processing.Genes & development · 2017Article
- Article
- 3' terminal diversity of MRP RNA and other human noncoding RNAs revealed by deep sequencing.BMC molecular biology · 2013Article
- Conserved regions of ribonucleoprotein ribonuclease MRP are involved in interactions with its substrate.Nucleic acids research · 2013Article
- Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy.Nucleic acids research · 2012Article
- Characterization of RNase MRP RNA and novel snoRNAs from Giardia intestinalis and Trichomonas vaginalis.BMC genomics · 2011Article
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
RNase MRP is a eukaryotic endoribonuclease involved in nucleolar and mitochondrial RNA processing events. RNase MRP is a ribonucleoprotein particle, which is structurally related to RNase P, an endoribonuclease involved in pre-tRNA processing. Most of the protein components of RNase MRP have been reported to be associated with RNase P as well. In this study we determined the association of these protein subunits with the human RNase MRP and RNase P particles by glycerol gradient sedimentation and coimmunoprecipitation. In agreement with previous studies, RNase MRP sedimented at 12S and 60-80S. In contrast, only a single major peak was observed for RNase P at 12S. The analysis of individual protein subunits revealed that hPop4 (also known as Rpp29), Rpp21, Rpp20, and Rpp25 only sedimented in 12S fractions, whereas hPop1, Rpp40, Rpp38, and Rpp30 were also found in 60-80S fractions. In agreement with their cosedimentation with RNase P RNA in the 12S peak, coimmunoprecipitation with VSV-epitope-tagged protein subunits revealed that hPop4, Rpp21, and in addition Rpp14 preferentially associate with RNase P. These data show that hPop4, Rpp21, and Rpp14 may not be associated with RNase MRP. Furthermore, Rpp20 and Rpp25 appear to be associated with only a subset of RNase MRP particles, in contrast to hPop1, Rpp40, Rpp38, and Rpp30 (and possibly also hPop5), which are probably associated with all RNase MRP complexes. Our data are consistent with a transient association of Rpp20 and Rpp25 with RNase MRP, which may be inversely correlated to its involvement in pre-rRNA processing.
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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.