Structure of PTB Bound to RNA: Specific Binding and Implications for Splicing Regulation

Author:

Oberstrass Florian C.1234,Auweter Sigrid D.1234,Erat Michèle1234,Hargous Yann1234,Henning Anke1234,Wenter Philipp1234,Reymond Luc1234,Amir-Ahmady Batoul1234,Pitsch Stefan1234,Black Douglas L.1234,Allain Frédéric H.-T.1234

Affiliation:

1. Institute for Molecular Biology and Biophysics, Department of Biology, Swiss Federal Institute of Technology, Zürich, ETH-Hönggerberg, CH-8093 Zürich, Switzerland.

2. Department of Microbiology, Immunology, and Molecular Genetics and Howard Hughes Medical Institute, University of California Los Angeles, Los Angeles, CA 90095, USA.

3. Laboratory of Nucleic Acid Chemistry LCAN-EPFL, Lausanne, Switzerland.

4. Molecular Life Science Ph.D. Program, Zürich, Switzerland.

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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