Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD

Mineyuki Mizuguchi; Takayuki Obita; Asagi Kajiyama; Yuki Kozakai; Tsuyoshi Nakai; Yuko Nabeshima; Hitoshi Okazawa

doi:10.1002/1873-3468.12256

Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD

Mineyuki Mizuguchi^*, Takayuki Obita, Asagi Kajiyama, Yuki Kozakai, Tsuyoshi Nakai, Yuko Nabeshima, Hitoshi Okazawa

^*Corresponding author for this work

Structural Biology

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

8 Scopus citations

Abstract

Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.

Original language	English
Pages (from-to)	2221-2231
Number of pages	11
Journal	FEBS Letters
DOIs	https://doi.org/10.1002/1873-3468.12256
State	Published - 2016/07/01

Keywords

allosteric mechanism
interaction
intrinsically disordered protein

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD",

abstract = "Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.",

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author = "Mineyuki Mizuguchi and Takayuki Obita and Asagi Kajiyama and Yuki Kozakai and Tsuyoshi Nakai and Yuko Nabeshima and Hitoshi Okazawa",

note = "Publisher Copyright: {\textcopyright} 2016 Federation of European Biochemical Societies",

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doi = "10.1002/1873-3468.12256",

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T1 - Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD

AU - Mizuguchi, Mineyuki

AU - Obita, Takayuki

AU - Kajiyama, Asagi

AU - Kozakai, Yuki

AU - Nakai, Tsuyoshi

AU - Nabeshima, Yuko

AU - Okazawa, Hitoshi

PY - 2016/7/1

Y1 - 2016/7/1

N2 - Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.

AB - Polyglutamine tract-binding protein 1 (PQBP1) is an intrinsically disordered protein composed of a small folded WW domain and a long disordered region. PQBP1 binds to spliceosomal proteins WBP11 and U5-15kD through its N-terminal WW domain and C-terminal region, respectively. Here, we reveal that the binding between PQBP1 and WBP11 reduces the binding affinity between PQBP1 and U5-15kD. Our results suggest that the interaction between PQBP1 and WBP11 negatively modulates the U5-15kD binding of PQBP1 by an allosteric mechanism.

KW - allosteric mechanism

KW - interaction

KW - intrinsically disordered protein

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DO - 10.1002/1873-3468.12256

M3 - 学術論文

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SN - 0014-5793

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JO - FEBS Letters

JF - FEBS Letters

ER -

Allosteric modulation of the binding affinity between PQBP1 and the spliceosomal protein U5-15kD

Abstract

Keywords

ASJC Scopus subject areas

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