Comparative Genetics of the Poly-Q tract of ataxin-1 and its binding protein PQBP-1

Tatsuaki Kurosaki; Jun Gojobori; Shintaroh Ueda

doi:10.1007/s10528-011-9473-1

Comparative Genetics of the Poly-Q tract of ataxin-1 and its binding protein PQBP-1

Tatsuaki Kurosaki
, Jun Gojobori
, Shintaroh Ueda

Biotechnical and Clinical Laboratory Sciences

University at Buffalo

The Graduate University for Advanced Studies
The University of Tokyo

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

4 Scopus citations

Abstract

Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. The poly-Q tracts show extensive variation in both the number and the configuration of repeats among species. A surface plasmon resonance assay showed clear interaction between human PQBP-1 and Q ₁₁, representative of the poly-Q tract of the ataxin- 1 of Old World monkeys. No response was observed using Q ₂PQ ₂P ₄Q ₂, representative of the poly-Q tract of the ataxin-1 of New World monkeys. This implies that the interaction of human PQBP-1 with ataxin-1 is limited to humans and closely related species. Comparison of the human and mouse PQBP-1 sequences showed an elevated amino acid substitution rate in the polar amino acid-rich domain of PQBP-1 that is responsible for binding to poly-Q tracts. This could have been advantageous to the new biological function of human PQBP-1 through poly-Q tracts.

Original language	English
Pages (from-to)	309-317
Number of pages	9
Journal	Biochemical Genetics
Volume	50
Issue number	3-4
DOIs	https://doi.org/10.1007/s10528-011-9473-1
State	Published - Apr 2012

Keywords

Ataxin-1
Intrinsically disordered
Nonsynonymous substitution
PQBP-1
Poly-Q tract

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10.1007/s10528-011-9473-1

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title = "Comparative Genetics of the Poly-Q tract of ataxin-1 and its binding protein PQBP-1",

abstract = "Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. The poly-Q tracts show extensive variation in both the number and the configuration of repeats among species. A surface plasmon resonance assay showed clear interaction between human PQBP-1 and Q 11, representative of the poly-Q tract of the ataxin- 1 of Old World monkeys. No response was observed using Q 2PQ 2P 4Q 2, representative of the poly-Q tract of the ataxin-1 of New World monkeys. This implies that the interaction of human PQBP-1 with ataxin-1 is limited to humans and closely related species. Comparison of the human and mouse PQBP-1 sequences showed an elevated amino acid substitution rate in the polar amino acid-rich domain of PQBP-1 that is responsible for binding to poly-Q tracts. This could have been advantageous to the new biological function of human PQBP-1 through poly-Q tracts.",

keywords = "Ataxin-1, Intrinsically disordered, Nonsynonymous substitution, PQBP-1, Poly-Q tract",

author = "Tatsuaki Kurosaki and Jun Gojobori and Shintaroh Ueda",

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AU - Gojobori, Jun

AU - Ueda, Shintaroh

PY - 2012/4

Y1 - 2012/4

N2 - Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. The poly-Q tracts show extensive variation in both the number and the configuration of repeats among species. A surface plasmon resonance assay showed clear interaction between human PQBP-1 and Q 11, representative of the poly-Q tract of the ataxin- 1 of Old World monkeys. No response was observed using Q 2PQ 2P 4Q 2, representative of the poly-Q tract of the ataxin-1 of New World monkeys. This implies that the interaction of human PQBP-1 with ataxin-1 is limited to humans and closely related species. Comparison of the human and mouse PQBP-1 sequences showed an elevated amino acid substitution rate in the polar amino acid-rich domain of PQBP-1 that is responsible for binding to poly-Q tracts. This could have been advantageous to the new biological function of human PQBP-1 through poly-Q tracts.

AB - Human PQBP-1 is known to interact with triplet repeat disease gene products such as ataxin and huntingtin through their poly-glutamine (poly-Q) tracts. The poly-Q tracts show extensive variation in both the number and the configuration of repeats among species. A surface plasmon resonance assay showed clear interaction between human PQBP-1 and Q 11, representative of the poly-Q tract of the ataxin- 1 of Old World monkeys. No response was observed using Q 2PQ 2P 4Q 2, representative of the poly-Q tract of the ataxin-1 of New World monkeys. This implies that the interaction of human PQBP-1 with ataxin-1 is limited to humans and closely related species. Comparison of the human and mouse PQBP-1 sequences showed an elevated amino acid substitution rate in the polar amino acid-rich domain of PQBP-1 that is responsible for binding to poly-Q tracts. This could have been advantageous to the new biological function of human PQBP-1 through poly-Q tracts.

KW - Ataxin-1

KW - Intrinsically disordered

KW - Nonsynonymous substitution

KW - PQBP-1

KW - Poly-Q tract

UR - https://www.scopus.com/pages/publications/84862773377

U2 - 10.1007/s10528-011-9473-1

DO - 10.1007/s10528-011-9473-1

M3 - Article

C2 - 21964520

SN - 0006-2928

VL - 50

SP - 309

EP - 317

JO - Biochemical Genetics

JF - Biochemical Genetics

IS - 3-4

ER -

Comparative Genetics of the Poly-Q tract of ataxin-1 and its binding protein PQBP-1

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Keywords

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