PQBP-1/Npw38, a Nuclear Protein Binding to the Polyglutamine Tract, Interacts with U5-15kD/dim1p via the Carboxyl-Terminal Domain

PQBP-1 was identified as a binding protein to the polyglutamine tract present in various transcription-related factors and causative genes for neurodegenerative disorders. This novel gene contains at least two functional domains, WW domain and carboxyl-terminal domain (CTD), strictly conserved beyon...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2000-07, Vol.273 (2), p.592-595
Main Authors: Waragai, M., Junn, E., Kajikawa, M., Takeuchi, S., Kanazawa, I., Shibata, M., Mouradian, M.M., Okazawa, H.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Base Sequence
Binding Sites - genetics
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
DNA Primers - genetics
Humans
In Vitro Techniques
Mice
Molecular Sequence Data
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
Peptides - metabolism
Protein Structure, Tertiary - genetics
Sequence Homology, Amino Acid
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Summary:PQBP-1 was identified as a binding protein to the polyglutamine tract present in various transcription-related factors and causative genes for neurodegenerative disorders. This novel gene contains at least two functional domains, WW domain and carboxyl-terminal domain (CTD), strictly conserved beyond species. Although human PQBP-1 additionally contains the polar amino acid-rich domain by which it binds to the polyglutamine tract, genuine physiological function(s) have not been clarified. In this study, we showed that U5-15kD, human homologue of fission yeast dim1p, is a partner molecule of PQBP-1 binding to CTD. This finding suggests physiological functions of PQBP-1 in splicing, cell cycle, and ubiquitination, through which we can speculate the pathological roles of PQBP-1 in triplet repeat diseases.
ISSN:0006-291X
1090-2104
DOI:10.1006/bbrc.2000.2992