Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2000-8-29
pubmed:abstractText
Dentatorubral-pallidoluysian atrophy (DRPLA) is one of the hereditary neurodegenerative disorders caused by expansion of CAG/glutamine repeats. To investigate the normal function of the DRPLA gene and the pathogenic mechanism of neuron death in specific areas of the brain, we isolated and analyzed a gene that shares a notable motif with DRPLA, arginine-glutamic acid (RE) dipeptide repeats. The gene isolated, designated RERE, has an open reading frame of 1566 amino acids, of which the C-terminal portion has 67% homology to DRPLA, whereas the N-terminal portion is distinctive. RERE also contains arginine-aspartic acid (RD) dipeptide repeats and putative nuclear localization signal sequences, but no polyglutamine tracts. RERE is expressed at a low level in most tissues examined. Immunoprecipitation and in vitro binding assays demonstrate that the DRPLA and RERE proteins bind each other, for which one of the RE repeats has a primary role, and extended polyglutamine enhances the binding. With engineered constructs fused with a tag, the RERE protein localized predominantly in the nucleus. Moreover, when RERE is overexpressed, the distribution of endogenous DRPLA protein alters from the diffused to the speckled pattern in the nucleus so as to co-localize with RERE. More RERE protein is recruited into nuclear aggregates of the DRPLA protein with extended polyglutamine than into those of pure polyglutamine. These results reveal a function for the DRPLA protein in the nucleus and the RE repeat in the protein-protein interaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/Arginine, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Cross-Linking Reagents, http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary, http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid, http://linkedlifedata.com/resource/pubmed/chemical/Green Fluorescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Luminescent Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Nerve Tissue Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Peptides, http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins, http://linkedlifedata.com/resource/pubmed/chemical/atrophin-1, http://linkedlifedata.com/resource/pubmed/chemical/polyglutamine
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0964-6906
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1433-42
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10814707-Amino Acid Sequence, pubmed-meshheading:10814707-Arginine, pubmed-meshheading:10814707-Blotting, Western, pubmed-meshheading:10814707-Brain, pubmed-meshheading:10814707-Carrier Proteins, pubmed-meshheading:10814707-Cell Nucleus, pubmed-meshheading:10814707-Cross-Linking Reagents, pubmed-meshheading:10814707-Cytoplasm, pubmed-meshheading:10814707-DNA, Complementary, pubmed-meshheading:10814707-Glutamic Acid, pubmed-meshheading:10814707-Green Fluorescent Proteins, pubmed-meshheading:10814707-HeLa Cells, pubmed-meshheading:10814707-Humans, pubmed-meshheading:10814707-Luminescent Proteins, pubmed-meshheading:10814707-Molecular Sequence Data, pubmed-meshheading:10814707-Nerve Tissue Proteins, pubmed-meshheading:10814707-Open Reading Frames, pubmed-meshheading:10814707-Peptides, pubmed-meshheading:10814707-Plasmids, pubmed-meshheading:10814707-Precipitin Tests, pubmed-meshheading:10814707-Protein Binding, pubmed-meshheading:10814707-Recombinant Fusion Proteins, pubmed-meshheading:10814707-Sequence Homology, Amino Acid, pubmed-meshheading:10814707-Signal Transduction, pubmed-meshheading:10814707-Tissue Distribution, pubmed-meshheading:10814707-Transfection
pubmed:year
2000
pubmed:articleTitle
Protein binding of a DRPLA family through arginine-glutamic acid dipeptide repeats is enhanced by extended polyglutamine.
pubmed:affiliation
National Children's Medical Research Center, Setagaya, Tokyo 154-8509 Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't