Folding intermediate binds to the bottom of bullet-shaped holo-chaperonin and is readily accessible to antibody.
J Mol Biol
; 236(3): 691-6, 1994 Feb 25.
Article
em En
| MEDLINE
| ID: mdl-7906737
ABSTRACT
Holo-chaperonin from Thermus thermophilus (Thermus holo-cpn) is a bullet-shaped particle where chaperonin-10 heptamer locates at one axial end of the cylindrical body of chaperonin-60 tetradecamer. Thermus holo-cpn promotes in-vitro folding of denatured 3-isopropylmalate dehydrogenase (IPMDH) from the same bacterium. We observed the complexes of Thermus holo-cpn and folding intermediates of IPMDH by immuno-electron microscopy after decoration by single layer labeling with anti-IPMDH IgG or by double layer labeling with anti-IPMDH IgG as first layer and antibodies against IgG as second layer. Images of the electron microscope showed that anti-IPMDH IgG was bound to the bottom end of the bullet-shaped Thermus holo-cpn. This result provides direct evidence that the folding intermediate binds to the axial end, which is opposite to the end where chaperonin-10 heptamer resides, of the cylindrical body of chaperonin-60 tetradecamer, and that bound folding intermediate in the complex is sufficiently exposed to the outside to be accessible by antibody.
Buscar no Google
Base de dados:
MEDLINE
Assunto principal:
Thermus thermophilus
/
Dobramento de Proteína
/
Oxirredutases do Álcool
/
Proteínas de Choque Térmico
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article