Symmetric GroEL-GroES complexes can contain substrate simultaneously in both GroEL rings.
FEBS Lett
; 405(2): 195-9, 1997 Mar 24.
Article
en En
| MEDLINE
| ID: mdl-9089290
ABSTRACT
Incubation of rhodanese with hche aperonins GroEL and GroES (12 GroEL14GroES7 molar ratio) under functional and steady state conditions for ATP leads to the formation of a high proportion of rhodanese-bound symmetric complexes (GroEL14(GroES7)2), as revealed by native electrophoresis. Aliquots of such samples were observed under the electron microscope, and the symmetric particles were classified using neuronal networks and multivariate statistical analysis. Three different populations of symmetric particles were obtained which contained substrate in none, one or both GroEL cavities, respectively. The presence of substrate in the symmetric complexes under functional conditions supports their role as active intermediates in the protein folding cycle. These results also suggest that symmetric GroEL-GroES complexes can use both rings simultaneously for folding, probably increasing the efficiency of the reaction.
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Banco de datos:
MEDLINE
Asunto principal:
Tiosulfato Azufretransferasa
/
Pliegue de Proteína
/
Chaperonina 60
/
Chaperonina 10
Tipo de estudio:
Prognostic_studies
Idioma:
En
Año:
1997
Tipo del documento:
Article