Specificity of ribonucleoprotein interaction determined by RNA folding during complex formulation.
Nature
; 380(6575): 646-50, 1996 Apr 18.
Article
em En
| MEDLINE
| ID: mdl-8602269
ABSTRACT
Many proteins involved in pre-mRNA processing contain one or more copies of a 70-90-amino-acid alphabeta module called the ribonucleoprotein domain. RNA maturation depends on the specific recognition by ribonucleoproteins of RNA elements within pre-mRNAs and small nuclear RNAs. The human U1A protein binds an RNA hairpin during splicing, and regulates its own expression by binding an internal loop in the 3'-untranslated region of its pre-mRNA, preventing polyadenylation. Here we report the nuclear magnetic resonance structure of the complex between the regulatory element of the U1A 3'-untranslated region (UTR) and the U1A protein RNA-binding domain. Specific intermolecular recognition requires the interaction of the variable loops of the ribonucleoprotein domain with the well-structured helical regions of the RNA. Formation of the complex then orders the flexible RNA single-stranded loop against the protein beta-sheet surface, and reorganizes the carboxy-terminal region of the protein to maximize surface complementarity and functional group recognition.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
RNA
/
Proteínas de Ligação a RNA
/
Ribonucleoproteína Nuclear Pequena U1
Tipo de estudo:
Prognostic_studies
Limite:
Humans
Idioma:
En
Revista:
Nature
Ano de publicação:
1996
Tipo de documento:
Article
País de afiliação:
Reino Unido