Characterization of the 5 S RNA binding activity of Xenopus zinc finger protein p43.
J Mol Biol
; 245(5): 549-58, 1995 Feb 03.
Article
en En
| MEDLINE
| ID: mdl-7844825
ABSTRACT
One major component of the Xenopus 42 S ribonucleoprotein (RNP) storage particle is the p43 protein. The 5 S RNA binding protein is structurally similar to TFIIIA, containing nine zinc finger domains. The RNA binding properties of recombinant p43 were characterized using a nitrocellulose filter binding assay. The experimental conditions necessary for in vitro p43-5 S RNA complex formation include pH 7.5, 0.1 M KCl and incubation at 22 degrees C. Under these conditions, the protein binds to Xenopus oocyte 5 S RNA with an apparent association constant of 1.61(+/- 0.12) x 10(9) M-1. A series of mutations in 5 S RNA were used to determine which sequence and structural features of the 5 S RNA are required for high affinity binding of p43. The primary contact points for p43 include the sequences and structures of stems II, V and loop D of the 5 S RNA. Although p43 and TFIIIA are structurally similar and are both relatively insensitive to mutations in the 5 S RNA, they do require different features of the 5 S RNA molecule for high affinity binding.
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Base de datos:
MEDLINE
Asunto principal:
Proteínas Ribosómicas
/
Factores de Transcripción
/
ARN Ribosómico 5S
/
Dedos de Zinc
/
Proteínas de Unión al ARN
/
Proteínas de Xenopus
/
Proteínas de Unión al ADN
Límite:
Animals
Idioma:
En
Revista:
J Mol Biol
Año:
1995
Tipo del documento:
Article
País de afiliación:
Canadá