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GroEL and the GroEL-GroES Complex

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Macromolecular Protein Complexes

Part of the book series: Subcellular Biochemistry ((SCBI,volume 83))

Abstract

Chaperonin is categorized as a molecular chaperone and mediates the formation of the native conformation of proteins by first preventing folding during synthesis or membrane translocation and subsequently by mediating the step-wise ATP-dependent release that result in proper folding. In the GroEL-GroES complex, a single heptameric GroEL ring binds one GroES ring in the presence of ATP/ADP, in this vein, the double ring GroEL tetradecamer is present in two distinct types of GroEL-GroES complexes: asymmetric 1:1 “bullet”-shaped GroEL:GroES and symmetric 1:2 “football” (American football)-shaped GroEL:GroES2. There have been debates as to which complex is critical to the productive protein folding mediated by the GroEL-GroES complex, and how GroES coordinates with GroEL in the chaperonin reaction cycle in association with regulation by adenine nucleotides and through the interplay of substrate proteins. A lot of knowledge on chaperonins has been accumulating as if expanding as ripples spread around the GroEL-GroES from Escherichia coli. In this article, an overview is presented on GroEL and the GroEL-GroES complex, with emphasis on their morphological variations, and some potential applications to the fabrication of nanocomposites using GroEL as a nano-block. In parallel, a guideline is presented that supports the recognition that the E. coli and its GroEL-GroES complex do not always receive in standard literature because the biochemical features of chaperonins derived from others special, such as mammals, are not always the same as those confirmed using GroEL-GroES derived from E. coli.

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Acknowledgements

The author would like to express thanks to the book editor, Professor Dr. Robin Harris for giving him this precious opportunity to review the progress thus far made on the Group I chaperonins , GroEL and the GroEL-GroES complexes research and to introduce some interdisciplinary applications using GroEL as a building nano-block, which forms the basis of a collaboration with Professor Dr. Takuzo Aida. The author’s appreciation is directed to him and his group members. He also appreciates Dr. Kenneth S. Kim for critical reading of the draft stage of the article.

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  1. Biomedical Research Institute, Department of Life Science and Biotechnology, National Institute of Advanced Industrial Science and Technology (AIST), Tsukuba Central-6, 1-1-1 Higashi Tsukuba Ibaraki, 305-8566, Tsukuba, Japan

    Noriyuki Ishii

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  1. Noriyuki Ishii
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Correspondence to Noriyuki Ishii .

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Editors and Affiliations

  1. Institute of Zoology, University of Mainz, Mainz, Germany

    J. Robin Harris

  2. School of Biology, Newcastle University, Newcastle upon Tyne, United Kingdom

    Jon Marles-Wright

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Ishii, N. (2017). GroEL and the GroEL-GroES Complex. In: Harris, J., Marles-Wright, J. (eds) Macromolecular Protein Complexes. Subcellular Biochemistry, vol 83. Springer, Cham. https://doi.org/10.1007/978-3-319-46503-6_17

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