The enigmatic RNase MRP of kinetoplastids. [PDF]
The ribonucleoprotein RNase MRP is responsible for the processing of ribosomal RNA precursors. It is found in virtually all eukaryotes that have been examined. In the Euglenozoa, including the genera Euglena, Diplonema and kinetoplastids, MRP RNA and protein subunits have so far escaped detection using bioinformatic methods. However, we now demonstrate
Alm Rosenblad M +2 more
europepmc +7 more sources
Reversible proliferative arrest induced by rapid depletion of RNase MRP [PDF]
Cellular quiescence is a state of reversible proliferative arrest that plays essential roles in development, resistance to stress, aging, and longevity of organisms.
Yuan Liu +9 more
doaj +4 more sources
A disease-linked lncRNA mutation in RNase MRP inhibits ribosome synthesis [PDF]
Mutations in the non-coding RNA RMRP cause primary immunodeficiency. Robertson et al show that a disease-associated mutation in RMRP impairs pre-ribosomal RNA processing and reduces ribosome abundance, establishing this disorder as a ribosomopathy.
Nic Robertson +7 more
doaj +4 more sources
Cryo-EM structure of catalytic ribonucleoprotein complex RNase MRP [PDF]
Ribozyme-based RNase MRP is an essential eukaryotic enzyme involved in the maturation of rRNA and is evolutionarily related to RNase P. Here, the authors present the 3.0 Å cryo-EM structure of the S.
Anna Perederina +6 more
doaj +5 more sources
RNase MRP cleaves pre-tRNASer-Met in the tRNA maturation pathway. [PDF]
Ribonuclease mitochondrial RNA processing (RNase MRP) is a multifunctional ribonucleoprotein (RNP) complex that is involved in the maturation of various types of RNA including ribosomal RNA.
Yuichiro Saito +8 more
doaj +4 more sources
Modular architecture of eukaryotic RNase P and RNase MRP revealed by electron microscopy. [PDF]
Ribonuclease P (RNase P) and RNase MRP are closely related ribonucleoprotein enzymes, which process RNA substrates including tRNA precursors for RNase P and 5.8 S rRNA precursors, as well as some mRNAs, for RNase MRP. The structures of RNase P and RNase MRP have not yet been solved, so it is unclear how the proteins contribute to the structure of the ...
Hipp K +4 more
europepmc +8 more sources
Characterization of RNase MRP RNA and novel snoRNAs from Giardia intestinalis and Trichomonas vaginalis [PDF]
Background Eukaryotic cells possess a complex network of RNA machineries which function in RNA-processing and cellular regulation which includes transcription, translation, silencing, editing and epigenetic control.
Chen Xiaowei S +2 more
doaj +4 more sources
Composition and RNA binding specificity of metazoan RNase MRP. [PDF]
Abstract Ribonuclease (RNase) MRP is a conserved RNA-based enzyme best known for its essential role in the maturation of ribosomal RNA (rRNA) in eukaryotes. However, the composition and RNA substrate specificity of this multisubunit ribonucleoprotein complex in higher eukaryotes remain a mystery.
Liu Y +9 more
europepmc +7 more sources
A Novel Method to Isolate RNase MRP Using RNA Streptavidin Aptamer Tags [PDF]
Interactions between RNA-binding proteins and RNA molecules are at the center of multiple biological processes. Therefore, accurate characterization of the composition of ribonucleoprotein complexes (RNPs) is crucial.
Violette Charteau +2 more
doaj +2 more sources
A novel experimental approach for the selective isolation and characterization of human RNase MRP [PDF]
RNase MRP is a ribonucleoprotein complex involved in the endoribonucleolytic cleavage of different RNAs. Mutations in the RNA component of the RNP are the cause of cartilage hair hypoplasia.
Merel Derksen +5 more
doaj +2 more sources

