| pubmed-article:10352175 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:10352175 | lifeskim:mentions | umls-concept:C1167298 | lld:lifeskim |
| pubmed-article:10352175 | lifeskim:mentions | umls-concept:C0073243 | lld:lifeskim |
| pubmed-article:10352175 | lifeskim:mentions | umls-concept:C0599220 | lld:lifeskim |
| pubmed-article:10352175 | lifeskim:mentions | umls-concept:C0165198 | lld:lifeskim |
| pubmed-article:10352175 | pubmed:issue | 12 | lld:pubmed |
| pubmed-article:10352175 | pubmed:dateCreated | 1999-7-26 | lld:pubmed |
| pubmed-article:10352175 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10352175 | pubmed:abstractText | RNase MRP is a ribonucleoprotein particle involved in the processing of pre-rRNA. The RNase MRP particle is structurally highly related to the RNase P particle, which is involved in pre-tRNA processing. Their RNA components fold into a similar secondary structure and they share several protein subunits. We have identified and characterised human and mouse cDNAs that encode proteins homologous to yPop4p, a protein subunit of both the yeast RNase MRP and RNase P complexes. The human Pop4 cDNA encodes a highly basic protein of 220 amino acids. Transfection experiments with epitope-tagged hPop4 protein indicated that hPop4 is localised in the nucleus and accumulates in the nucleolus. Immunoprecipitation assays using extracts from transfected cells expressing epitope-tagged hPop4 revealed that this protein is associated with both the human RNase MRP and RNase P particles. Polyclonal rabbit antibodies raised against recombinant hPop4 recognised a 30 kDa protein in total HeLa cell extracts and specifically co-immunoprecipitated the RNA components of the RNase MRP and RNase P complexes. Finally we showed that anti-hPop4 immunoprecipitates possess RNase P enzymatic activity. Taken together, these data show that we have identified a protein that represents the human counterpart of the yeast Pop4p protein. | lld:pubmed |
| pubmed-article:10352175 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10352175 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10352175 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10352175 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10352175 | pubmed:month | Jun | lld:pubmed |
| pubmed-article:10352175 | pubmed:issn | 0305-1048 | lld:pubmed |
| pubmed-article:10352175 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:10352175 | pubmed:author | pubmed-author:PruijnG JGJ | lld:pubmed |
| pubmed-article:10352175 | pubmed:author | pubmed-author:van... | lld:pubmed |
| pubmed-article:10352175 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10352175 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10352175 | pubmed:volume | 27 | lld:pubmed |
| pubmed-article:10352175 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10352175 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10352175 | pubmed:pagination | 2465-72 | lld:pubmed |
| pubmed-article:10352175 | pubmed:dateRevised | 2008-11-20 | lld:pubmed |
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| pubmed-article:10352175 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10352175 | pubmed:articleTitle | hPop4: a new protein subunit of the human RNase MRP and RNase P ribonucleoprotein complexes. | lld:pubmed |
| pubmed-article:10352175 | pubmed:affiliation | Department of Biochemistry, University of Nijmegen, PO Box 9101, NL-6500 HB Nijmegen, The Netherlands. | lld:pubmed |
| pubmed-article:10352175 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10352175 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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