Ligand-Induced Reassembly of GroEL/ES Chaperone In Vitro: Visualization by Electron Microscopy
- Authors: Ryabova N.A.1, Selivanova O.M.1, Semisotnov G.V.1
-
Affiliations:
- Institute of Protein Research
- Issue: Vol 52, No 1 (2018)
- Pages: 103-107
- Section: Structural Functional Analysis of Biopolymers and Their Complexes
- URL: https://journals.rcsi.science/0026-8933/article/view/163426
- DOI: https://doi.org/10.1134/S0026893318010168
- ID: 163426
Cite item
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 onering 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.
About the authors
N. A. Ryabova
Institute of Protein Research
Email: nina@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
O. M. Selivanova
Institute of Protein Research
Email: nina@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
G. V. Semisotnov
Institute of Protein Research
Author for correspondence.
Email: nina@vega.protres.ru
Russian Federation, Pushchino, Moscow oblast, 142290
Supplementary files
