| pubmed-article:21199950 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C0032098 | lld:lifeskim |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C0035701 | lld:lifeskim |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C1419408 | lld:lifeskim |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C0073249 | lld:lifeskim |
| pubmed-article:21199950 | lifeskim:mentions | umls-concept:C1257755 | lld:lifeskim |
| pubmed-article:21199950 | pubmed:issue | 3 | lld:pubmed |
| pubmed-article:21199950 | pubmed:dateCreated | 2011-1-19 | lld:pubmed |
| pubmed-article:21199950 | pubmed:abstractText | RNase T2 enzymes are conserved in most eukaryotic genomes, and expression patterns and phylogenetic analyses suggest that they may carry out an important housekeeping role. However, the nature of this role has been elusive. Here we show that RNS2, an intracellular RNase T2 from Arabidopsis thaliana, is essential for normal ribosomal RNA recycling. This enzyme is the main endoribonuclease activity in plant cells and localizes to the endoplasmic reticulum (ER), ER-derived structures, and vacuoles. Mutants lacking RNS2 activity accumulate RNA intracellularly, and rRNA in these mutants has a longer half-life. Normal rRNA turnover seems essential to maintain cell homeostasis because rns2 mutants display constitutive autophagy. We propose that RNS2 is part of a process that degrades rRNA to recycle its components. This process appears to be conserved in all eukaryotes. | lld:pubmed |
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| pubmed-article:21199950 | pubmed:language | eng | lld:pubmed |
| pubmed-article:21199950 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21199950 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:21199950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21199950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:21199950 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:21199950 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:21199950 | pubmed:month | Jan | lld:pubmed |
| pubmed-article:21199950 | pubmed:issn | 1091-6490 | lld:pubmed |
| pubmed-article:21199950 | pubmed:author | pubmed-author:ContentoAntho... | lld:pubmed |
| pubmed-article:21199950 | pubmed:author | pubmed-author:BasshamDiane... | lld:pubmed |
| pubmed-article:21199950 | pubmed:author | pubmed-author:MeyerAlexande... | lld:pubmed |
| pubmed-article:21199950 | pubmed:author | pubmed-author:HillwigMeliss... | lld:pubmed |
| pubmed-article:21199950 | pubmed:author | pubmed-author:MacintoshGust... | lld:pubmed |
| pubmed-article:21199950 | pubmed:author | pubmed-author:EbanyDanielle... | lld:pubmed |
| pubmed-article:21199950 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:21199950 | pubmed:day | 18 | lld:pubmed |
| pubmed-article:21199950 | pubmed:volume | 108 | lld:pubmed |
| pubmed-article:21199950 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:21199950 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:21199950 | pubmed:pagination | 1093-8 | lld:pubmed |
| pubmed-article:21199950 | pubmed:dateRevised | 2011-8-1 | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:meshHeading | pubmed-meshheading:21199950... | lld:pubmed |
| pubmed-article:21199950 | pubmed:year | 2011 | lld:pubmed |
| pubmed-article:21199950 | pubmed:articleTitle | RNS2, a conserved member of the RNase T2 family, is necessary for ribosomal RNA decay in plants. | lld:pubmed |
| pubmed-article:21199950 | pubmed:affiliation | Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA 50011, USA. | lld:pubmed |
| pubmed-article:21199950 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:21199950 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:21199950 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| entrez-gene:818563 | entrezgene:pubmed | pubmed-article:21199950 | lld:entrezgene |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:21199950 | lld:entrezgene |
