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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
1996-2-13
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/DNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NOP1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Transfer,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Helicases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Ligase (ATP),
http://linkedlifedata.com/resource/pubmed/chemical/RNA Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, Small Nucleolar,
http://linkedlifedata.com/resource/pubmed/chemical/SEN1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/SSB1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0026-8925
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
20
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pubmed:volume |
249
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
571-84
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:8544822-Amino Acid Sequence,
pubmed-meshheading:8544822-Biological Transport,
pubmed-meshheading:8544822-Cell Compartmentation,
pubmed-meshheading:8544822-Cell Nucleolus,
pubmed-meshheading:8544822-Cell Nucleus,
pubmed-meshheading:8544822-DNA Helicases,
pubmed-meshheading:8544822-Fluorescent Antibody Technique, Indirect,
pubmed-meshheading:8544822-Fungal Proteins,
pubmed-meshheading:8544822-Genes, Fungal,
pubmed-meshheading:8544822-HSP70 Heat-Shock Proteins,
pubmed-meshheading:8544822-Molecular Sequence Data,
pubmed-meshheading:8544822-Mutation,
pubmed-meshheading:8544822-Nuclear Proteins,
pubmed-meshheading:8544822-RNA, Transfer,
pubmed-meshheading:8544822-RNA Helicases,
pubmed-meshheading:8544822-RNA Ligase (ATP),
pubmed-meshheading:8544822-RNA Precursors,
pubmed-meshheading:8544822-RNA Splicing,
pubmed-meshheading:8544822-Ribonucleoproteins, Small Nucleolar,
pubmed-meshheading:8544822-Saccharomyces cerevisiae,
pubmed-meshheading:8544822-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:8544822-Sequence Deletion,
pubmed-meshheading:8544822-Structure-Activity Relationship
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pubmed:year |
1995
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pubmed:articleTitle |
Inactivation of the yeast Sen1 protein affects the localization of nucleolar proteins.
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pubmed:affiliation |
Laboratory of Genetics, University of Wisconsin, Madison 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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