A peptide motif in Raver1 mediates splicing repression by interaction with the PTB RRM2 domain.
Nat Struct Mol Biol
; 13(9): 839-48, 2006 Sep.
Article
em En
| MEDLINE
| ID: mdl-16936729
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.
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Base de dados:
MEDLINE
Assunto principal:
Proteínas Nucleares
/
Proteínas de Transporte
/
Splicing de RNA
/
Proteína de Ligação a Regiões Ricas em Polipirimidinas
Idioma:
En
Ano de publicação:
2006
Tipo de documento:
Article