pubmed-article:10864042 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C0205145 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C1330957 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C0596311 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C1704666 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C1517892 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C0028608 | lld:lifeskim |
pubmed-article:10864042 | lifeskim:mentions | umls-concept:C0208973 | lld:lifeskim |
pubmed-article:10864042 | pubmed:issue | 6 | lld:pubmed |
pubmed-article:10864042 | pubmed:dateCreated | 2000-7-17 | lld:pubmed |
pubmed-article:10864042 | pubmed:abstractText | Chemical modifications and processing of the 18S, 5.8S, and 25S ribosomal RNAs from the 35S pre-ribosomal RNA depend on an important set of small nucleolar ribonucleoprotein particles (snoRNPs). Genetic depletion of yeast Gar1p, an essential common component of H/ACA snoRNPs, leads to inhibition of uridine isomerizations to pseudo-uridines on the 35S pre-rRNA and of the early pre-rRNA cleavages at sites A1 and A2, resulting in a loss of mature 18S rRNA synthesis. To identify Gar1p functional partners, we screened for mutations that are synthetically lethal with a gar1 mutant allele encoding a Gar1p mutant protein lacking its two glycine/arginine-rich (GAR) domains. We identified a previously uncharacterized Saccharomyces cerevisiae open reading frame, YDR083W (now designated RRP8), that encodes a highly conserved protein containing motifs found in methyltransferases. Rrp8p localizes to the nucleolus. A yeast strain lacking this protein is viable at 30 degrees C but displays strong growth impairment at lower temperatures. In this strain, cleavage of the pre-rRNA at site A2 is strongly affected whereas cleavages at sites A0 and A1 are only slightly inhibited or delayed. | lld:pubmed |
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pubmed-article:10864042 | pubmed:language | eng | lld:pubmed |
pubmed-article:10864042 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:10864042 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:10864042 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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