Effectors increase the affinity of ADP-ribosylation factor for GTP to increase binding.

Zhu, X; Boman, A L; Kuai, J; Cieplak, W; Kahn, R A

Zhu, X; Boman, A L; Kuai, J; Cieplak, W; Kahn, R A.

Afiliación

Zhu X; Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322-3050, USA.

J Biol Chem ; 275(18): 13465-75, 2000 May 05.

Article en En | MEDLINE | ID: mdl-10788460

RESUMEN

The stoichiometry of the binding of GTP to ADP-ribosylation factor (ARF) proteins, normally quite low at approximately 0.05 mol/mol protein, was found to increase to a maximum of 1 mol/mol in the presence of effectors. The mechanism of this action was found to result from the ability of these effectors to increase the affinity of ARF for activating guanine nucleotide triphosphates. The existence of a conformation of ARF with low affinity (>100 micrometer) for GTP is proposed. The actions of effectors to increase the equilibrium binding of GTP is interpreted as evidence that these same effectors interact with and modulate the affinity of the inactive ARF for GTP. A new model for these interactions among ARF, effectors, and GTP is proposed, and a preliminary test in cells is supportive of these observations with relevance to signaling in cells.

Asunto(s)

Factores de Ribosilacion-ADP/química; Guanosina Trifosfato/química; Factores de Ribosilacion-ADP/metabolismo; Animales; Guanosina Trifosfato/metabolismo; Unión Proteica; Conformación Proteica; Ratas; Proteínas Recombinantes/química; Proteínas Recombinantes/metabolismo; Transducción de Señal

Buscar en Google

Añadir a Mi BVS

Imprimir

XML

PubMed Links

Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Factores de Ribosilacion-ADP / Guanosina Trifosfato Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: J Biol Chem Año: 2000 Tipo del documento: Article País de afiliación: Estados Unidos Pais de publicación: Estados Unidos

Buscar en Google

Añadir a Mi BVS

Imprimir

XML

PubMed Links