Ferritin Assembly Revisited: A Time-Resolved Small-Angle X-ray Scattering Study.
Biochemistry
; 55(2): 287-93, 2016 Jan 19.
Article
en En
| MEDLINE
| ID: mdl-26690025
ABSTRACT
The assembly reaction of Escherichia coli ferritin A (EcFtnA) was studied using time-resolved small-angle X-ray scattering (TR-SAXS). EcFtnA forms a cagelike structure that consists of 24 identical subunits and dissociates into dimers at acidic pH. The dimer maintains nativelike secondary and tertiary structures and is able to reassemble into a 24-mer when the pH is increased. The reassembly reaction was induced by pH jump, and reassembly was followed by TR-SAXS. Time-dependent changes in the forward scattering intensity and in the gyration radius suggested the existence of a significant population of intermediate oligomers during the assembly reaction. The initial reaction was a mixture of second- and third-order reactions (formation of tetramers and hexamers) from the protein concentration dependence of the initial velocity. The time-dependent change in the SAXS profile was roughly explained by a simple model in which only tetramers, hexamers, and dodecamers were considered as intermediates.
Texto completo:
1
Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Difracción de Rayos X
/
Dispersión del Ángulo Pequeño
/
Ferritinas
Idioma:
En
Revista:
Biochemistry
Año:
2016
Tipo del documento:
Article
País de afiliación:
Japón