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[Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy].
Ryabova, N A; Selivanova, O M; Semisotnov, G V.
Afiliación
  • Ryabova NA; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.
  • Selivanova OM; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.
  • Semisotnov GV; Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow oblast, 142290 Russia.
Mol Biol (Mosk) ; 52(1): 120-124, 2018.
Article en Ru | MEDLINE | ID: mdl-29512644
ABSTRACT
The products of the reassembly reaction of tetradecameric two-ring quaternary structure of GroEL chaperonin under the pressure of its heptameric co-chaperonin GroES have been visualized by electron microscopy. It has been shown that one-ring heptameric oligomers of GroEL have been formed at the beginning (after ~5 min) of the reaction, while at the final stage of the reaction (after ~70 min), both one-ring heptamers in complex with one GroES and two-rings tetradecamers in complexes with one (asymmetrical complex) or two (symmetrical complex) GroES heptamers are present. The relationship between the data of light scattering, native electrophoresis, and electron microscopy obtained earlier has been discussed.
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Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Chaperonina 60 / Chaperonina 10 / Proteínas de Escherichia coli / Escherichia coli Idioma: Ru Año: 2018 Tipo del documento: Article

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Chaperonina 60 / Chaperonina 10 / Proteínas de Escherichia coli / Escherichia coli Idioma: Ru Año: 2018 Tipo del documento: Article