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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1991-10-11
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pubmed:abstractText |
We have purified two major polypeptides of 54 and 56 kd from bovine erythrocytes that specifically bind the nuclear location sequence (NLS) of the SV40 large T antigen. When added to a permeabilized cell system for nuclear import, the purified proteins increase by 2- to 3-fold the nuclear accumulation of a fluorescent protein containing the large T antigen NLS. The import stimulation is saturable and dependent upon the presence of cytosol. Nuclear protein accumulation in vitro is sensitive to inactivation by N-ethylmaleimide (NEM). NEM inactivation can be overcome by addition of the purified NLS-binding proteins to the import system. NEM treatment of the purified proteins abolishes their ability to stimulate import but does not affect NLS binding. Our results indicate that the NLS-binding proteins are NEM-sensitive receptors for nuclear import. At least one other NEM-sensitive cytosolic activity and an NEM-insensitive cytosolic activity are also necessary for protein import in vitro.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, Polyomavirus Transforming,
http://linkedlifedata.com/resource/pubmed/chemical/Ethylmaleimide,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Cell Surface
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
0092-8674
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
66
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
837-47
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:1653647-Amino Acid Sequence,
pubmed-meshheading:1653647-Animals,
pubmed-meshheading:1653647-Antigens, Polyomavirus Transforming,
pubmed-meshheading:1653647-Binding Sites,
pubmed-meshheading:1653647-Biological Transport,
pubmed-meshheading:1653647-Cattle,
pubmed-meshheading:1653647-Cell Compartmentation,
pubmed-meshheading:1653647-Cell Nucleus,
pubmed-meshheading:1653647-Cytoplasm,
pubmed-meshheading:1653647-Ethylmaleimide,
pubmed-meshheading:1653647-Molecular Sequence Data,
pubmed-meshheading:1653647-Nuclear Proteins,
pubmed-meshheading:1653647-Peptides,
pubmed-meshheading:1653647-Protein Binding,
pubmed-meshheading:1653647-Receptors, Cell Surface,
pubmed-meshheading:1653647-Solubility
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pubmed:year |
1991
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pubmed:articleTitle |
Cytosolic proteins that specifically bind nuclear location signals are receptors for nuclear import.
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pubmed:affiliation |
Department of Cell, Molecular and Structural Biology, Northwestern University Medical School, Chicago, Illinois 60611.
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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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