Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain

Masaki Takahashi; Mineyuki Mizuguchi; Hiroyuki Shinoda; Tomoyasu Aizawa; Makoto Demura; Hitoshi Okazawa; Keiichi Kawano

doi:10.1016/j.bbapap.2010.03.007

Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain

Masaki Takahashi, Mineyuki Mizuguchi^*, Hiroyuki Shinoda, Tomoyasu Aizawa, Makoto Demura, Hitoshi Okazawa, Keiichi Kawano

^*Corresponding author for this work

Structural Biology

Research output: Contribution to journal › Article › peer-review

19 Scopus citations

Abstract

Polyglutamine tract-binding protein-1 (PQBP-1) is a nuclear protein that interacts with various proteins, including RNA polymerase II and the spliceosomal protein U5-15kD. PQBP-1 is known to be associated with X-linked mental retardation in which a frameshift mutation in the PQBP-1 gene occurs. In the present study, we demonstrate that PQBP-1 binds to U5-15kD via a continuous 23-residue segment within its C-terminal domain. Intriguingly, this segment is lost in the frameshift mutants of PQBP-1 associated with X-linked mental retardation. These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD.

Original language	English
Pages (from-to)	1500-1507
Number of pages	8
Journal	Biochimica et Biophysica Acta - Proteins and Proteomics
Volume	1804
Issue number	7
DOIs	https://doi.org/10.1016/j.bbapap.2010.03.007
State	Published - 2010/07

Keywords

PQBP-1
Polyglutamine
Protein structure
U5-15kD
Unstructured protein

ASJC Scopus subject areas

Analytical Chemistry
Biophysics
Biochemistry
Molecular Biology

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10.1016/j.bbapap.2010.03.007

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@article{1f609c4c5aec43dcb587df76829f9bd4,

title = "Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain",

abstract = "Polyglutamine tract-binding protein-1 (PQBP-1) is a nuclear protein that interacts with various proteins, including RNA polymerase II and the spliceosomal protein U5-15kD. PQBP-1 is known to be associated with X-linked mental retardation in which a frameshift mutation in the PQBP-1 gene occurs. In the present study, we demonstrate that PQBP-1 binds to U5-15kD via a continuous 23-residue segment within its C-terminal domain. Intriguingly, this segment is lost in the frameshift mutants of PQBP-1 associated with X-linked mental retardation. These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD.",

keywords = "PQBP-1, Polyglutamine, Protein structure, U5-15kD, Unstructured protein",

author = "Masaki Takahashi and Mineyuki Mizuguchi and Hiroyuki Shinoda and Tomoyasu Aizawa and Makoto Demura and Hitoshi Okazawa and Keiichi Kawano",

note = "Funding Information: This study was supported by Grants-in-Aid for Scientific Research on Innovative Areas (Research in a Proposed Research Area) from the Ministry of Education, Culture, Science and Technology of Japan . ",

year = "2010",

month = jul,

doi = "10.1016/j.bbapap.2010.03.007",

language = "英語",

volume = "1804",

pages = "1500--1507",

journal = "Biochimica et Biophysica Acta - Proteins and Proteomics",

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TY - JOUR

T1 - Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain

AU - Takahashi, Masaki

AU - Mizuguchi, Mineyuki

AU - Shinoda, Hiroyuki

AU - Aizawa, Tomoyasu

AU - Demura, Makoto

AU - Okazawa, Hitoshi

AU - Kawano, Keiichi

N1 - Funding Information: This study was supported by Grants-in-Aid for Scientific Research on Innovative Areas (Research in a Proposed Research Area) from the Ministry of Education, Culture, Science and Technology of Japan .

PY - 2010/7

Y1 - 2010/7

N2 - Polyglutamine tract-binding protein-1 (PQBP-1) is a nuclear protein that interacts with various proteins, including RNA polymerase II and the spliceosomal protein U5-15kD. PQBP-1 is known to be associated with X-linked mental retardation in which a frameshift mutation in the PQBP-1 gene occurs. In the present study, we demonstrate that PQBP-1 binds to U5-15kD via a continuous 23-residue segment within its C-terminal domain. Intriguingly, this segment is lost in the frameshift mutants of PQBP-1 associated with X-linked mental retardation. These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD.

AB - Polyglutamine tract-binding protein-1 (PQBP-1) is a nuclear protein that interacts with various proteins, including RNA polymerase II and the spliceosomal protein U5-15kD. PQBP-1 is known to be associated with X-linked mental retardation in which a frameshift mutation in the PQBP-1 gene occurs. In the present study, we demonstrate that PQBP-1 binds to U5-15kD via a continuous 23-residue segment within its C-terminal domain. Intriguingly, this segment is lost in the frameshift mutants of PQBP-1 associated with X-linked mental retardation. These findings suggest that the frameshift mutations in the PQBP-1 gene lead to expression of mutants lacking the ability to interact with U5-15kD.

KW - PQBP-1

KW - Polyglutamine

KW - Protein structure

KW - U5-15kD

KW - Unstructured protein

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U2 - 10.1016/j.bbapap.2010.03.007

DO - 10.1016/j.bbapap.2010.03.007

M3 - 学術論文

C2 - 20307692

AN - SCOPUS:77952319537

SN - 1570-9639

VL - 1804

SP - 1500

EP - 1507

JO - Biochimica et Biophysica Acta - Proteins and Proteomics

JF - Biochimica et Biophysica Acta - Proteins and Proteomics

IS - 7

ER -

Polyglutamine tract-binding protein-1 binds to U5-15kD via a continuous 23-residue segment of the C-terminal domain

Abstract

Keywords

ASJC Scopus subject areas

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