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 journalArticle

274 Citations (Scopus)

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 languageEnglish (US)
Pages (from-to)2054-2057
Number of pages4
JournalScience
Volume309
Issue number5743
DOIs
StatePublished - Sep 23 2005
Externally publishedYes

Fingerprint

Polypyrimidine Tract-Binding Protein
RNA
RNA-Binding Proteins
Structural Models
Alternative Splicing
Oligonucleotides
Exons
Messenger RNA

ASJC Scopus subject areas

  • General

Cite this

Oberstrass, F. C., Auwetor, S. D., Erat, M., Hargous, Y., Henning, A., Wenter, P., ... Allain, F. H. T. (2005). Structural biology - Structure of PTB bound to RNA: Specific binding and implications for splicing regulation. Science, 309(5743), 2054-2057. https://doi.org/10.1126/science.1114066

Structural biology - Structure of PTB bound to RNA : Specific binding and implications for splicing regulation. / Oberstrass, Florian C.; Auwetor, Sigrid D.; Erat, Michèle; Hargous, Yann; Henning, Anke; Wenter, Philipp; Reymond, Luc; Amir-Ahmady, Batoul; Pitsch, Stefan; Black, Douglas L.; Allain, Frédéric H.T.

In: Science, Vol. 309, No. 5743, 23.09.2005, p. 2054-2057.

Research output: Contribution to journalArticle

Oberstrass, FC, Auwetor, SD, Erat, M, Hargous, Y, Henning, A, Wenter, P, Reymond, L, Amir-Ahmady, B, Pitsch, S, Black, DL & Allain, FHT 2005, 'Structural biology - Structure of PTB bound to RNA: Specific binding and implications for splicing regulation', Science, vol. 309, no. 5743, pp. 2054-2057. https://doi.org/10.1126/science.1114066
Oberstrass, Florian C. ; Auwetor, Sigrid D. ; Erat, Michèle ; Hargous, Yann ; Henning, Anke ; Wenter, Philipp ; Reymond, Luc ; Amir-Ahmady, Batoul ; Pitsch, Stefan ; Black, Douglas L. ; Allain, Frédéric H.T. / Structural biology - Structure of PTB bound to RNA : Specific binding and implications for splicing regulation. In: Science. 2005 ; Vol. 309, No. 5743. pp. 2054-2057.
@article{24293fa01947482a8ef8345213fab907,
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.}",
year = "2005",
month = "9",
day = "23",
doi = "10.1126/science.1114066",
language = "English (US)",
volume = "309",
pages = "2054--2057",
journal = "Science",
issn = "0036-8075",
publisher = "American Association for the Advancement of Science",
number = "5743",

}

TY - JOUR

T1 - Structural biology - Structure of PTB bound to RNA

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

N2 - 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.

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.

UR - http://www.scopus.com/inward/record.url?scp=25444486174&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=25444486174&partnerID=8YFLogxK

U2 - 10.1126/science.1114066

DO - 10.1126/science.1114066

M3 - Article

C2 - 16179478

AN - SCOPUS:25444486174

VL - 309

SP - 2054

EP - 2057

JO - Science

JF - Science

SN - 0036-8075

IS - 5743

ER -