Source:http://linkedlifedata.com/resource/pubmed/id/14960378
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
3
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| pubmed:dateCreated |
2004-2-12
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| pubmed:abstractText |
The nuclear pore complex (NPC) controls transport of macromolecules across the nuclear envelope. It is large and complex but appears to consist of only approximately 30 different proteins despite its mass of > 60MDa. Vertebrate NPC structure has been analyzed by several methods giving a comprehensive architectural model. Despite our knowledge of yeast nucleoporins, structural data is more limited and suggests the basic organization is similar to vertebrates, but may lack some peripheral and other components. Using field emission scanning electron microscopy to probe NPC structure we found that the yeast, like higher eukaryotic, NPCs contain similar peripheral components. We can detect cytoplasmic rings and evidence of nucleoplasmic rings in yeasts. A filamentous basket is present on the nucleoplasmic face and evidence for cytoplasmic filaments is shown. We observed a central structure, possibly the transporter, that which may be linked to the cytoplasmic ring by internal filaments. Immuno-gold labeling suggested that Nup159p may be attached to the cytoplasmic ring, whereas Nup116p may be associated, partly, with the cytoplasmic filaments. Analysis of a Nup57p mutant suggested a role in maintaining the stability of cytoplasmic components of the NPC. We conclude that peripheral NPC components appear similar in yeasts compared to higher organisms and present a revised model for yeast NPC structural composition.
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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/NUP116 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/NUP159 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/NUP57 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Pore Complex Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Mar
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| pubmed:issn |
1047-8477
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
145
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
272-88
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| pubmed:dateRevised |
2009-6-10
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| pubmed:meshHeading |
pubmed-meshheading:14960378-Animals,
pubmed-meshheading:14960378-Cell Nucleus,
pubmed-meshheading:14960378-Chironomidae,
pubmed-meshheading:14960378-Cytoplasm,
pubmed-meshheading:14960378-Immunohistochemistry,
pubmed-meshheading:14960378-Microscopy, Electron, Scanning,
pubmed-meshheading:14960378-Models, Biological,
pubmed-meshheading:14960378-Mutation,
pubmed-meshheading:14960378-Nuclear Pore,
pubmed-meshheading:14960378-Nuclear Pore Complex Proteins,
pubmed-meshheading:14960378-Protein Conformation,
pubmed-meshheading:14960378-Ribosomes,
pubmed-meshheading:14960378-Saccharomyces cerevisiae,
pubmed-meshheading:14960378-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:14960378-Salivary Glands,
pubmed-meshheading:14960378-Schizosaccharomyces,
pubmed-meshheading:14960378-Temperature,
pubmed-meshheading:14960378-Xenopus
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| pubmed:year |
2004
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| pubmed:articleTitle |
Yeast nuclear pore complexes have a cytoplasmic ring and internal filaments.
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| pubmed:affiliation |
Structural Cell Biology, Paterson Institute for Cancer Research, Christie Hospital NHS Trust, Manchester M20 4BX, UK. m.w.goldberg@durham.ac.uk
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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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