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- Title
A peptide motif in Raver1 mediates splicing repression by interaction with the PTB RRM2 domain.
- Authors
Rideau, Alexis P.; Gooding, Clare; Simpson, Peter J.; Monie, Tom P.; Lorenz, Mike; Hüttelmaier, Stefan; Singer, Robert H.; Matthews, Stephen; Curry, Stephen; Smith, Christopher W. J.
- Abstract
Polypyrimidine tract–binding protein (PTB) is a regulatory splicing repressor. Raver1 acts as a PTB corepressor for splicing of α-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.
- Subjects
GENETIC engineering; PEPTIDES; CARRIER proteins; GENETIC repressors; MUTAGENESIS
- Publication
Nature Structural & Molecular Biology, 2006, Vol 13, Issue 9, p839
- ISSN
1545-9993
- Publication type
Article
- DOI
10.1038/nsmb1137