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Determination of functional domains in polypyrimidine-tract-binding protein.
Oh, Y L; Hahm, B; Kim, Y K; Lee, H K; Lee, J W; Song, O; Tsukiyama-Kohara, K; Kohara, M; Nomoto, A; Jang, S K.
Afiliación
  • Oh YL; Department of Life Science, Pohang University of Science and Technology, San31, Hyoja-Dong, Pohang, Kyungbuk 790-784, South Korea.
Biochem J ; 331 ( Pt 1): 169-75, 1998 Apr 01.
Article en En | MEDLINE | ID: mdl-9512476
ABSTRACT
Polypyrimidine-tract-binding protein (PTB) is involved in pre-mRNA splicing and internal-ribosomal-entry-site-dependent translation. The biochemical properties of various segments of PTB were analysed in order to understand the molecular basis of the PTB functions. The protein exists in oligomeric as well as monomeric form. The central part of PTB (amino acids 169-293) plays a major role in the oligomerization. PTB contains several RNA-binding motifs. Among them, the C-terminal part of PTB (amino acids 329-530) exhibited the strongest RNA-binding activity. The N-terminal part of PTB is responsible for the enhancement of RNA binding by HeLa cell cytoplasmic factor(s).
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribonucleoproteínas / ARN / Proteínas de Unión al ARN Límite: Humans Idioma: En Revista: Biochem J Año: 1998 Tipo del documento: Article País de afiliación: Corea del Sur

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Ribonucleoproteínas / ARN / Proteínas de Unión al ARN Límite: Humans Idioma: En Revista: Biochem J Año: 1998 Tipo del documento: Article País de afiliación: Corea del Sur