A peptide motif in Raver1 mediates splicing repression by interaction with the 
PTB RRM2 domain

Rideau, Alexis P; Gooding, Clare; Simpson, Peter J; Monie, Tom P; Lorenz, Mike; Huttelmaier, Stefan; Singer, Robert H; Matthews, Stephen; Curry, Stephen; Smith, Christopher W J

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A peptide motif in Raver1 mediates splicing repression by interaction with the PTB RRM2 domain

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Lorenz, Mike
Max Planck Institute of Molecular Cell Biology and Genetics, Max Planck Society;

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Citation

Rideau, A. P., Gooding, C., Simpson, P. J., Monie, T. P., Lorenz, M., Huttelmaier, S., et al. (2006). A peptide motif in Raver1 mediates splicing repression by interaction with the PTB RRM2 domain. Nature Structure and Molecular Biology, 13(9), 839-848.

Cite as: https://hdl.handle.net/21.11116/0000-0001-1007-5

Abstract

Polypyrimidine tract-binding protein (PTB) is a regulatory splicing repressor. Raver1 acts as a PTB corepressor for splicing of alpha-tropomyosin (Tpm1) exon 3. Here we define a minimal region of Raver1 that acts as a repressor domain when recruited to RNA. A conserved [S/G][I/L]LGxxP motif is essential for splicing repressor activity and sufficient for interaction with PTB. An adjacent proline-rich region is also essential for repressor activity but not for PTB interaction. NMR analysis shows that LLGxxP peptides interact with a hydrophobic groove on the dorsal surface of the RRM2 domain of PTB, which constitutes part of the minimal repressor region of PTB. The requirement for the PTB-Raver1 interaction that we have characterized may serve to bring the additional repressor regions of both proteins into a configuration that allows them to synergistically effect exon skipping.