Structural biology - Structure of PTB bound to RNA: Specific binding and implications for splicing regulation

Florian C. Oberstrass; Sigrid D. Auwetor; Michèle Erat; Yann Hargous; Anke Henning; Philipp Wenter; Luc Reymond; Batoul Amir-Ahmady; Stefan Pitsch; Douglas L. Black; Frédéric H.T. Allain

doi:10.1126/science.1114066

Structural biology - Structure of PTB bound to RNA: Specific binding and implications for splicing regulation

Florian C. Oberstrass, Sigrid D. Auwetor, Michèle Erat, Yann Hargous, Anke Henning, Philipp Wenter, Luc Reymond, Batoul Amir-Ahmady, Stefan Pitsch, Douglas L. Black, Frédéric H.T. Allain

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

360 Scopus citations

Abstract

The polypyrimidine tract binding protein (PTB) is a 58-kilodalton RNA binding protein involved in multiple aspects of messenger RNA metabolism, including the repression of alternative exons. We have determined the solution structures of the four RNA binding domains (RBDs) of PTB, each bound to a CUCUCU oligonucleotide. Each RBD binds RNA with a different binding specificity. RBD3 and RBD4 interact, resulting in an antiparallel orientation of their bound RNAs. Thus, PTB will induce RNA looping when bound to two separated pyrimidine tracts within the same RNA. This leads to structural models for how PTB functions as an alternative-splicing repressor.

Original language	English (US)
Pages (from-to)	2054-2057
Number of pages	4
Journal	Science
Volume	309
Issue number	5743
DOIs	https://doi.org/10.1126/science.1114066
State	Published - Sep 23 2005
Externally published	Yes

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title = "Structural biology - Structure of PTB bound to RNA: Specific binding and implications for splicing regulation",

abstract = "The polypyrimidine tract binding protein (PTB) is a 58-kilodalton RNA binding protein involved in multiple aspects of messenger RNA metabolism, including the repression of alternative exons. We have determined the solution structures of the four RNA binding domains (RBDs) of PTB, each bound to a CUCUCU oligonucleotide. Each RBD binds RNA with a different binding specificity. RBD3 and RBD4 interact, resulting in an antiparallel orientation of their bound RNAs. Thus, PTB will induce RNA looping when bound to two separated pyrimidine tracts within the same RNA. This leads to structural models for how PTB functions as an alternative-splicing repressor.",

author = "Oberstrass, {Florian C.} and Auwetor, {Sigrid D.} and Mich{\`e}le Erat and Yann Hargous and Anke Henning and Philipp Wenter and Luc Reymond and Batoul Amir-Ahmady and Stefan Pitsch and Black, {Douglas L.} and Allain, {Fr{\'e}d{\'e}ric H.T.}",

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doi = "10.1126/science.1114066",

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T2 - Specific binding and implications for splicing regulation

AU - Oberstrass, Florian C.

AU - Auwetor, Sigrid D.

AU - Erat, Michèle

AU - Hargous, Yann

AU - Henning, Anke

AU - Wenter, Philipp

AU - Reymond, Luc

AU - Amir-Ahmady, Batoul

AU - Pitsch, Stefan

AU - Black, Douglas L.

AU - Allain, Frédéric H.T.

PY - 2005/9/23

Y1 - 2005/9/23

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AB - The polypyrimidine tract binding protein (PTB) is a 58-kilodalton RNA binding protein involved in multiple aspects of messenger RNA metabolism, including the repression of alternative exons. We have determined the solution structures of the four RNA binding domains (RBDs) of PTB, each bound to a CUCUCU oligonucleotide. Each RBD binds RNA with a different binding specificity. RBD3 and RBD4 interact, resulting in an antiparallel orientation of their bound RNAs. Thus, PTB will induce RNA looping when bound to two separated pyrimidine tracts within the same RNA. This leads to structural models for how PTB functions as an alternative-splicing repressor.

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Structural biology - Structure of PTB bound to RNA: Specific binding and implications for splicing regulation

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