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

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

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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