Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1993-3-16
pubmed:abstractText
We have generated temperature-sensitive lethal point mutations in the small nucleolar RNA-associated protein fibrillarin (encoded by the NOP1 gene in yeast) and analyzed their effects on ribosome synthesis. The five alleles tested all prevent synthesis of normal ribosomes, but in dramatically different ways. At the non-permissive temperature, the nop1.2 and nop1.5 alleles prevent synthesis of both 18S and 25S rRNA and all pre-rRNA species except the 35S primary transcript. In contrast, the nop1.3, nop1.4, and nop1.7 alleles do not strongly impair processing. In nop1.3 strains, nucleolar methylation of pre-rRNA is strongly inhibited; late, cytoplasmic methylation of 18S rRNA and tRNA methylation continue. The nop1.4 and nop1.7 alleles result in the synthesis of cytoplasmic 60S ribosomal subunits with strongly aberrant mobilities on sucrose gradients even at the permissive temperature, owing to the impairment of a late step in ribosome assembly. Thus, all major posttranscriptional activities in ribosome synthesis, pre-rRNA processing, pre-rRNA modification, and ribosome assembly are dependent on fibrillarin.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0092-8674
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
72
pubmed:geneSymbol
NOP1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
443-57
pubmed:dateRevised
2000-12-18
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Temperature-sensitive mutations demonstrate roles for yeast fibrillarin in pre-rRNA processing, pre-rRNA methylation, and ribosome assembly.
pubmed:affiliation
European Molecular Biology Laboratory, Heidelberg, Germany.
pubmed:publicationType
Journal Article