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

Florian C. Oberstrass(Howard Hughes Medical Institute), Sigrid Auweter(Howard Hughes Medical Institute), Michèle C. Erat(Howard Hughes Medical Institute), Yann Hargous(Howard Hughes Medical Institute), A Henning(Howard Hughes Medical Institute), Philipp Wenter(Howard Hughes Medical Institute), Luc Reymond(Howard Hughes Medical Institute), Batoul Amir-Ahmady(Howard Hughes Medical Institute), Stefan Pitsch(Howard Hughes Medical Institute), Douglas L. Black(Howard Hughes Medical Institute), Frédéric H.‐T. Allain(Howard Hughes Medical Institute)
Science
September 22, 2005
Cited by 464

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.


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