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rdf:type | |
lifeskim:mentions | |
pubmed:dateCreated |
1998-2-5
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pubmed:abstractText |
Rat7p/Nup159p is an essential nucleoporin of Sac-charomyces cerevisiae originally isolated in a genetic screen designed to identify yeast temperature-sensitive mutants defective in mRNA export. Here we describe a detailed structural-functional analysis of Rat7p/Nup159p. The mutation in the rat7-1 ts allele, isolated in the original genetic screen, was found to be a single base pair change that created a stop codon approximately 100 amino acids upstream of the actual stop codon of this 1,460 amino acid polypeptide, thus eliminating one of the two predicted coiled-coil regions located near the carboxyl terminus of the protein. These coiled-coil regions are essential since an allele lacking both coiled-coil regions was unable to support growth under any conditions. In contrast, no other region of the protein was absolutely required. The SAFG/PSFG repeat region in the central third of the protein was completely dispensable for growth at temperatures between 16 degrees C and 37 degrees C and cells expressing this mutant allele were indistinguishable from wild type. Deletion of the amino-terminal third of the protein, upstream from the repeat region, or the portion between the repeat region and the coiled-coils resulted in temperature-sensitivity, but the two alleles showed distinct phenotypes with respect to the behavior of nuclear pore complexes (NPCs). Taken together, our data suggest that Rat7p/Nup159p is anchored within the NPC through its coiled-coil region and adjacent sequences. In addition, we postulate that the N-terminal third of Rat7p/Nup159p plays an important role in mRNA export.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/NUP159 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Fungal,
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 |
0021-9533
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
110 ( Pt 23)
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2987-99
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9359887-Alleles,
pubmed-meshheading:9359887-Amino Acid Substitution,
pubmed-meshheading:9359887-Fungal Proteins,
pubmed-meshheading:9359887-Genes, Fungal,
pubmed-meshheading:9359887-Kinetics,
pubmed-meshheading:9359887-Membrane Proteins,
pubmed-meshheading:9359887-Mutagenesis, Site-Directed,
pubmed-meshheading:9359887-Nuclear Pore Complex Proteins,
pubmed-meshheading:9359887-Nuclear Proteins,
pubmed-meshheading:9359887-Polymerase Chain Reaction,
pubmed-meshheading:9359887-RNA, Fungal,
pubmed-meshheading:9359887-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:9359887-Saccharomyces cerevisiae,
pubmed-meshheading:9359887-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:9359887-Sequence Deletion
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pubmed:year |
1997
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pubmed:articleTitle |
A structure/function analysis of Rat7p/Nup159p, an essential nucleoporin of Saccharomyces cerevisiae.
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pubmed:affiliation |
Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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