Spectroscopic studies on the mode of binding of ATP, UTP and alpha-amanitin with yeast RNA polymerase II.
FEBS Lett
; 241(1-2): 33-7, 1988 Dec 05.
Article
em En
| MEDLINE
| ID: mdl-3058514
ABSTRACT
The binding affinity between the substrates ATP and UTP with the purified yeast RNA polymerase II have been studied here in the presence and absence of Mn2+. In the absence of template DNA, both ATP and UTP showed tight binding with the enzyme without preference for any specific nucleotide, unlike Escherichia coli RNA polymerase. Fluorescence titration of the tryptophan emission of the enzyme by nucleoside triphosphate substrates gave an estimated Kd value around 65 microM in the absence of Mn2+ whereas in the presence of Mn2+, the Kd was 20 microM. The effect of substrates on the longitudinal relaxation of the HDO proton in enzyme-substrate complex also yielded a similar Kd value.
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Base de dados:
MEDLINE
Assunto principal:
Nucleotídeos de Uracila
/
Uridina Trifosfato
/
RNA Polimerase II
/
Trifosfato de Adenosina
/
Amanitinas
Idioma:
En
Revista:
FEBS Lett
Ano de publicação:
1988
Tipo de documento:
Article
País de afiliação:
Índia