ArticleMolecular biology of the cell2001
Basic domains target protein subunits of the RNase MRP complex to the nucleolus independently of complex association.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
9 citing papers in PubMed, 27 citations in OpenAlex.
- Footprinting analysis demonstrates extensive similarity between eukaryotic RNase P and RNase MRP holoenzymes.RNA (New York, N.Y.) · 2008Article
- Human RNase P: a tRNA-processing enzyme and transcription factor.Nucleic acids research · 2007Review
- Evolutionary comparison provides evidence for pathogenicity of RMRP mutations.PLoS genetics · 2005Article
- Nonphosphorylated human La antigen interacts with nucleolin at nucleolar sites involved in rRNA biogenesis.Molecular and cellular biology · 2004Article
- Role of pre-rRNA base pairing and 80S complex formation in subnucleolar localization of the U3 snoRNP.Molecular and cellular biology · 2004Article
- Alterations in the intracellular level of a protein subunit of human RNase P affect processing of tRNA precursors.Nucleic acids research · 2003Article
- Coordinated nuclear export of 60S ribosomal subunits and NMD3 in vertebrates.The EMBO journal · 2003Article
- The human La (SS-B) autoantigen interacts with DDX15/hPrp43, a putative DEAH-box RNA helicase.RNA (New York, N.Y.) · 2002Article
- An active precursor in assembly of yeast nuclear ribonuclease P.RNA (New York, N.Y.) · 2002Article
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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
The RNase MRP and RNase P ribonucleoprotein particles both function as endoribonucleases, have a similar RNA component, and share several protein subunits. RNase MRP has been implicated in pre-rRNA processing and mitochondrial DNA replication, whereas RNase P functions in pre-tRNA processing. Both RNase MRP and RNase P accumulate in the nucleolus of eukaryotic cells. In this report we show that for three protein subunits of the RNase MRP complex (hPop1, hPop4, and Rpp38) basic domains are responsible for their nucleolar accumulation and that they are able to accumulate in the nucleolus independently of their association with the RNase MRP and RNase P complexes. We also show that certain mutants of hPop4 accumulate in the Cajal bodies, suggesting that hPop4 traverses through these bodies to the nucleolus. Furthermore, we characterized a deletion mutant of Rpp38 that preferentially associates with the RNase MRP complex, giving a first clue about the difference in protein composition of the human RNase MRP and RNase P complexes. On the basis of all available data on nucleolar localization sequences, we hypothesize that nucleolar accumulation of proteins containing basic domains proceeds by diffusion and retention rather than by an active transport process. The existence of nucleolar localization sequences is discussed.
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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.