| pubmed-article:8544822 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:8544822 | lifeskim:mentions | umls-concept:C0043393 | lld:lifeskim |
| pubmed-article:8544822 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8544822 | lifeskim:mentions | umls-concept:C0001721 | lld:lifeskim |
| pubmed-article:8544822 | lifeskim:mentions | umls-concept:C1423721 | lld:lifeskim |
| pubmed-article:8544822 | lifeskim:mentions | umls-concept:C0475264 | lld:lifeskim |
| pubmed-article:8544822 | lifeskim:mentions | umls-concept:C0028608 | lld:lifeskim |
| pubmed-article:8544822 | pubmed:issue | 6 | lld:pubmed |
| pubmed-article:8544822 | pubmed:dateCreated | 1996-2-13 | lld:pubmed |
| pubmed-article:8544822 | pubmed:abstractText | A mutation in the Saccharomyces cerevisiae SEN1 gene causes accumulation of end-matured, intron-containing pre-tRNAs. Cells containing the thermosensitive sen1-1 mutation exhibit reduced tRNA splicing endonuclease activity. However, Sen1p is not the catalytic subunit of this enzyme. We have used Sen1p-specific antibodies for cell fractionation studies and immunofluorescent microscopy and determined that Sen1p is a low abundance protein of about 239 kDa. It localizes to the nucleus with a granular distribution. We verified that a region in SEN1 containing a putative nuclear localization signal sequence (NLS) is necessary for nuclear targeting. Furthermore, we found that inactivation of Sen1p by temperature shift of a strain carrying sen1-1 leads to mislocalization of two nucleolar proteins, Nop1 and Ssb1. Possible mechanisms are discussed for several related nuclear functions of Sen1p, including tRNA splicing and the maintenance of a normal crescent-shaped nucleolus. | lld:pubmed |
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| pubmed-article:8544822 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:8544822 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:8544822 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8544822 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8544822 | pubmed:issn | 0026-8925 | lld:pubmed |
| pubmed-article:8544822 | pubmed:author | pubmed-author:CulbertsonM... | lld:pubmed |
| pubmed-article:8544822 | pubmed:author | pubmed-author:UrsicDD | lld:pubmed |
| pubmed-article:8544822 | pubmed:author | pubmed-author:DeMariniD JDJ | lld:pubmed |
| pubmed-article:8544822 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8544822 | pubmed:day | 20 | lld:pubmed |
| pubmed-article:8544822 | pubmed:volume | 249 | lld:pubmed |
| pubmed-article:8544822 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8544822 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8544822 | pubmed:pagination | 571-84 | lld:pubmed |
| pubmed-article:8544822 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:8544822 | pubmed:year | 1995 | lld:pubmed |
| pubmed-article:8544822 | pubmed:articleTitle | Inactivation of the yeast Sen1 protein affects the localization of nucleolar proteins. | lld:pubmed |
| pubmed-article:8544822 | pubmed:affiliation | Laboratory of Genetics, University of Wisconsin, Madison 53706, USA. | lld:pubmed |
| pubmed-article:8544822 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8544822 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:8544822 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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