Interaction of BiP with substance P and nucleotides.
Cell Mol Biol Res
; 41(5): 397-403, 1995.
Article
em En
| MEDLINE
| ID: mdl-8867787
ABSTRACT
A rapid and simple spin column assay has been used to study interactions of BiP with substance P (SP) and ATP. At 4 degrees C, the binding of SP to BiP requires ATP and a stable SP-BiP.ATP complex is formed. Nonhydrolyzable ATP analogues or ADP cannot replace ATP. Although ATP converts BiP dimers to monomers, the requirement for ATP for SP binding is not solely due to BiP dissociation, because purified BiP monomers also require ATP for peptide binding. At 37 degrees C, there is rapid binding of SP to BiP even in the absence of ATP and, in fact, ATP at concentrations above 5 microM causes release of SP from BiP. At this higher temperature, there is also rapid hydrolysis of ATP bound to BiP. These results extend our previous results (Brot et al., 1994) that indicated the formation, at low ATP concentrations, of a labile SP.BiP.ATP complex that, after ATP hydrolysis, resulted in a stable SP.BiP.ADP complex.
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Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Proteínas de Transporte
/
Substância P
/
Trifosfato de Adenosina
/
Chaperonas Moleculares
/
Proteínas de Choque Térmico
Idioma:
En
Revista:
Cell Mol Biol Res
Assunto da revista:
BIOLOGIA MOLECULAR
Ano de publicação:
1995
Tipo de documento:
Article
País de afiliação:
Estados Unidos