PMID- 11032753
OWN - NLM
STAT- MEDLINE
DCOM- 20001130
LR  - 20211203
IS  - 0006-291X (Print)
IS  - 0006-291X (Linking)
VI  - 277
IP  - 2
DP  - 2000 Oct 22
TI  - The CUG-binding protein binds specifically to UG dinucleotide repeats in a yeast 
      three-hybrid system.
PG  - 518-23
AB  - The CUG-binding protein (CUG-BP) has been reported to be involved in the 
      pathogenesis of myotonic dystrophy (DM) through binding to a CUG trinucleotide 
      repeat located in the 3' untranslated region (3'UTR) of the DM protein kinase 
      (DMPK) gene. We found that CUG-BP associates with long CUG trinucleotide repeats 
      ((CUG)(11)(CUG)(12)), but not with short repeats ((CUG)(12)) in a yeast 
      three-hybrid system. On the other hand, CUG-BP+LYLQ, an alternatively spliced 
      isoform of CUG-BP, does not associate with CUG trinucleotide repeats regardless 
      of the repeat length. In addition to these findings, we found that CUG-BP and 
      CUG-BP+LYLQ strongly and specifically associate with UG dinucleotide repeats. 
      Deletion analyse of CUG-BP revealed that the absence of the first or third 
      RNA-binding domain (RBD I and RBD III, respectively) does not affect the 
      interaction between CUG-BP and UG dinucleotide repeats. Loss of the second 
      RNA-binding domain (RBD II) decreases the affinity of CUG-BP for UG dinucleotide 
      repeats by about 40%. Unexpectedly, deletion of the linker domain most severely 
      reduces the interaction, although this region does not contain a known 
      RNA-binding motif. Our results suggest the possibility that both CUG-BP and 
      CUG-BP+LYLQ associate with UG repeat-containing mRNAs and regulate such metabolic 
      properties as mRNA localization, stability, and translation, and provide new 
      insights into the pathogenesis of DM.
CI  - Copyright 2000 Academic Press.
FAU - Takahashi, N
AU  - Takahashi N
AD  - Department of Life Sciences, Graduate School of Arts and Sciences, University of 
      Tokyo, 3-8-1 Komaba, Meguro-ku, Tokyo, 153-8902, Japan.
FAU - Sasagawa, N
AU  - Sasagawa N
FAU - Suzuki, K
AU  - Suzuki K
FAU - Ishiura, S
AU  - Ishiura S
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biochem Biophys Res Commun
JT  - Biochemical and biophysical research communications
JID - 0372516
RN  - 0 (3' Untranslated Regions)
RN  - 0 (CELF1 Protein)
RN  - 0 (CELF1 protein, human)
RN  - 0 (DMPK protein, human)
RN  - 0 (Oligonucleotides)
RN  - 0 (Protein Isoforms)
RN  - 0 (RNA-Binding Proteins)
RN  - 0 (Ribonucleoproteins)
RN  - EC 2.7.11.1 (Myotonin-Protein Kinase)
RN  - EC 2.7.11.1 (Protein Serine-Threonine Kinases)
RN  - EC 3.2.1.23 (beta-Galactosidase)
SB  - IM
MH  - 3' Untranslated Regions
MH  - Alternative Splicing
MH  - CELF1 Protein
MH  - Dinucleotide Repeats
MH  - Gene Deletion
MH  - Mutagenesis, Site-Directed
MH  - Myotonin-Protein Kinase
MH  - Oligonucleotides/metabolism
MH  - Plasmids/metabolism
MH  - Protein Binding
MH  - Protein Isoforms
MH  - Protein Serine-Threonine Kinases/metabolism
MH  - Protein Structure, Tertiary
MH  - RNA-Binding Proteins/*metabolism
MH  - Ribonucleoproteins/*metabolism
MH  - Saccharomyces cerevisiae/metabolism
MH  - Two-Hybrid System Techniques
MH  - beta-Galactosidase/metabolism
EDAT- 2000/10/18 11:00
MHDA- 2001/02/28 10:01
CRDT- 2000/10/18 11:00
PHST- 2000/10/18 11:00 [pubmed]
PHST- 2001/02/28 10:01 [medline]
PHST- 2000/10/18 11:00 [entrez]
AID - S0006-291X(00)93694-5 [pii]
AID - 10.1006/bbrc.2000.3694 [doi]
PST - ppublish
SO  - Biochem Biophys Res Commun. 2000 Oct 22;277(2):518-23. doi: 
      10.1006/bbrc.2000.3694.