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Papers In Press, published online ahead of print November 9, 2005
J. Biol. Chem, 10.1074/jbc.M510578200
Submitted on September 27, 2005
Revised on November 4, 2005
Accepted on November 9, 2005

A splicing repressor domain in polypyrimidine tract binding protein

Fiona Robinson and Christopher W. J. Smith

Biochemistry Dept., University of Cambridge, Cambridge CB2 1GA

Corresponding Author: cwjs1{at}cam.ac.uk

Polypyrimidine Tract Binding protein (PTB) is an hnRNP with four RRM type domains. It plays roles as a repressive alternative splicing regulator of multilple target genes, as well as being involved in pre-mRNA 3’ end processing, mRNA localization, stability and IRES-mediated translation. Here we have used a tethered function assay, in which a fusion protein of PTB and the bacteriophage MS2 coat protein is recruited to a splicing regulatory site by binding to an artificially inserted MS2 binding site. Deletion mutations of PTB in this system allowed us to identify RRM2 and the following inter-RRM linker region as the minimal region of PTB that can act as splicing repressor domain when recruited to RNA. Splicing repression by the minimal repressor domain remained cell-type specific and dependent upon other defined regulatory elements in the a-tropomyosin test minigene. Our results highlight the fact that splicing repression by PTB can be uncoupled from the mode by which it binds to RNA.


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