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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
5-6
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pubmed:dateCreated |
2000-3-28
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pubmed:abstractText |
The X-linked form of the bone marrow failure syndrome Dyskeratosis congenital is caused by mutations in dyskerin, a 514 amino acid protein that is presumed to play a role in ribosome biogenesis. Here we report that dyskerin tagged with the human immunoglobulin epitope localizes to nuclei of transfected HeLa and COS-1 cells. A carboxyl-terminal domain consisting of amino acids 467-475 and encoding KKEKKKSKK is both necessary and sufficient to mediate nuclear entry. Immunoglobulin-tagged dyskerin did not interact with the Fanconi anemia group A protein, FANCA. These results suggest a nuclear role for dyskerin. Moreover, hematopoietic failure observed in both Dyskeratosis congenital and the most common type of Fanconi anemia is unlikely to have a common mechanism resulting from abnormal physical interactions between the respective gene products of these disorders.
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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/Affinity Labels,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DKC1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/DNA-Binding Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/FANCA protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Fanconi Anemia Complementation...,
http://linkedlifedata.com/resource/pubmed/chemical/Immunoglobulin G,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Localization Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Nuclear Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins
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pubmed:status |
MEDLINE
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pubmed:issn |
1079-9796
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
25
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
305-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:10744426-Affinity Labels,
pubmed-meshheading:10744426-Animals,
pubmed-meshheading:10744426-COS Cells,
pubmed-meshheading:10744426-Cell Cycle Proteins,
pubmed-meshheading:10744426-DNA-Binding Proteins,
pubmed-meshheading:10744426-Dyskeratosis Congenita,
pubmed-meshheading:10744426-Epitopes,
pubmed-meshheading:10744426-Fanconi Anemia Complementation Group A Protein,
pubmed-meshheading:10744426-HeLa Cells,
pubmed-meshheading:10744426-Humans,
pubmed-meshheading:10744426-Immunoglobulin G,
pubmed-meshheading:10744426-Microscopy, Fluorescence,
pubmed-meshheading:10744426-Mutation,
pubmed-meshheading:10744426-Nuclear Localization Signals,
pubmed-meshheading:10744426-Nuclear Proteins,
pubmed-meshheading:10744426-Protein Binding,
pubmed-meshheading:10744426-Proteins,
pubmed-meshheading:10744426-Recombinant Fusion Proteins,
pubmed-meshheading:10744426-Subcellular Fractions,
pubmed-meshheading:10744426-Transfection
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pubmed:articleTitle |
Analysis of epitope-tagged forms of the dyskeratosis congenital protein (dyskerin): identification of a nuclear localization signal.
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pubmed:affiliation |
Department of Molecular and Human Genetics, Baylor College of Medicine.Houston. TX 77030, USA. hagopy@bcm.tmc.edu
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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