Involvement of a 50-kDa mRNP protein from Saccharomyces cerevisiae in mRNA binding to ribosomes.
Arch Biochem Biophys
; 344(1): 1-10, 1997 Aug 01.
Article
em En
| MEDLINE
| ID: mdl-9244375
A yeast 50-kDa mRNA-binding protein (50mRNP) is found selectively associated with the 48S and 80S initiation complexes. This protein is structurally related to the translational elongation factor EF-1alpha. The protein reacts with antibodies directed against EF-1alpha and, similarly, EF-1alpha recognizes antibodies against the 50mRNP protein. This is evidence that they share at least one epitope which allows a similar antigenic behavior. In addition, both proteins show similar cleavage patterns upon treatment with the endoproteinase Lys-C. A murine antibody raised against 50mRNP inhibits both 48S and 80S initiation complex formation. The inhibitory effect is relieved by preincubating anti-50mRNP with EF-1alpha. Antibody to EF-1alpha manifests a similar inhibitory pattern for the formation of 48S and 80S complexes. These data strongly suggest that 50mRNP is an EF-1alpha-like polypeptide essential for the formation of the above complexes.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Ribonucleoproteínas
/
Ribossomos
/
Saccharomyces cerevisiae
/
RNA Mensageiro
/
Proteínas de Ligação a RNA
Idioma:
En
Revista:
Arch Biochem Biophys
Ano de publicação:
1997
Tipo de documento:
Article
País de afiliação:
Venezuela
País de publicação:
Estados Unidos