The transcriptional activator GAL4-VP16 regulates the intra-molecular interactions of the TATA-binding protein.
J Biosci
;
2003 Jun; 28(4): 423-36
Artigo
em Inglês
| IMSEAR
| ID: sea-110783
ABSTRACT
Binding characteristics of yeast TATA-binding protein (yTBP) over five oligomers having different TATA variants and lacking a UASGAL, showed that TATA-binding protein (TBP)-TATA complex gets stabilized in the presence of the acidic activator GAL4-VP16. Activator also greatly suppressed the non-specific TBP-DNA complex formation. The effects were more pronounced over weaker TATA boxes. Activator also reduced the TBP dimer levels both in vitro and in vivo, suggesting the dimer may be a direct target of transcriptional activators. The transcriptional activator facilitated the dimer to monomer transition and activated monomers further to help TBP bind even the weaker TATA boxes stably. The overall stimulatory effect of the GAL4-VP16 on the TBP-TATA complex formation resembles the known effects of removal of the N-terminus of TBP on its activity, suggesting that the activator directly targets the N-terminus of TBP and facilitates its binding to the TATA box.
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Índice:
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Assunto principal:
Ligação Proteica
/
Fatores de Transcrição
/
DNA
/
Proteínas Fúngicas
/
Ativação Transcricional
/
Transativadores
/
Estrutura Terciária de Proteína
/
Proteína Vmw65 do Vírus do Herpes Simples
/
Dimerização
/
Reagentes de Ligações Cruzadas
Tipo de estudo:
Estudo prognóstico
Idioma:
Inglês
Revista:
J Biosci
Ano de publicação:
2003
Tipo de documento:
Artigo
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