Chaperonin GroEL uses asymmetric and symmetric reaction cycles in response to the concentration of non-native substrate proteins

• Iizuka Ryo

  Graduate School of Pharmaceutical Sciences, The University of Tokyo

• Funatsu Takashi

  Graduate School of Pharmaceutical Sciences, The University of Tokyo

抄録

The Escherichia coli chaperonin GroEL is an essential molecular chaperone that mediates protein folding in association with its cofactor, GroES. It is widely accepted that GroEL alternates the GroES-sealed folding-active rings during the reaction cycle. In other words, an asymmetric GroEL–GroES complex is formed during the cycle, whereas a symmetric GroEL–(GroES)₂ complex is not formed. However, this conventional view has been challenged by the recent reports indicating that such symmetric complexes can be formed in the GroEL–GroES reaction cycle. In this review, we discuss the studies of the symmetric GroEL–(GroES)₂ complex, focusing on the molecular mechanism underlying its formation. We also suggest that GroEL can be involved in two types of reaction cycles (asymmetric or symmetric) and the type of cycle used depends on the concentration of non-native substrate proteins.

収録刊行物

• Biophysics and Physicobiology

  Biophysics and Physicobiology 13 (0), 63-69, 2016

  一般社団法人 日本生物物理学会

キーワード

• molecular chaperone
• protein folding
• protein–protein interaction

詳細情報

• CRID: 1390282680741628672
• NII論文ID: 130005148429
• DOI: 10.2142/biophysico.13.0_63
• ISSN: 21894779
• Web Site: https://www.jstage.jst.go.jp/article/biophysico/13/0/13_63/_pdf
• 本文言語コード: en
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• 抄録ライセンスフラグ: 使用不可