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PQBP-1/Npw38, a nuclear protein binding to the polyglutamine tract, interacts with U5-15kD/dim1p via the carboxyl-terminal domain.

Abstract：

: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.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Waragai M,Junn E,Kajikawa M,Takeuchi S,Kanazawa I,Shibata M,Mouradian MM,Okazawa H

doi

10.1006/bbrc.2000.2992

subject

Has Abstract

pub_date

2000-07-05 00:00:00

pages

592-5

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(00)92992-9

journal_volume

273

pub_type

杂志文章

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