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Literature DB >> 11533646

Single-molecule observation of protein-protein interactions in the chaperonin system.

H Taguchi¹, T Ueno, H Tadakuma, M Yoshida, T Funatsu.

Abstract

We have analyzed the dynamics of the chaperonin (GroEL)-cochaperonin (GroES) interaction at the single-molecule level. In the presence of ATP and non-native protein, binding of GroES to the immobilized GroEL occurred at a rate that is consistent with bulk kinetics measurements. However, the release of GroES from GroEL occurred after a lag period ( approximately 3 s) that was not recognized in earlier bulk-phase studies. This observation suggests a new kinetic intermediate in the GroEL-GroES reaction pathway.

Entities: Chemical Gene

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Year: 2001 PMID： 11533646 DOI： 10.1038/nbt0901-861

Source DB: PubMed Journal: Nat Biotechnol ISSN： 1087-0156 Impact factor: 54.908

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Cited

31 in total

1. Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes.

Authors: Vananh T Nguyen; Yoshiyuki Kamio; Hideo Higuchi
Journal: EMBO J Date: 2003-10-01 Impact factor: 11.598

2. The interaction of beta(2)-glycoprotein I domain V with chaperonin GroEL: the similarity with the domain V and membrane interaction.

Authors: Masayo Gozu; Masaru Hoshino; Takashi Higurashi; Hisao Kato; Yuji Goto
Journal: Protein Sci Date: 2002-12 Impact factor: 6.725

3. Single-molecule spectroscopy of protein folding in a chaperonin cage.

Authors: Hagen Hofmann; Frank Hillger; Shawn H Pfeil; Armin Hoffmann; Daniel Streich; Dominik Haenni; Daniel Nettels; Everett A Lipman; Benjamin Schuler
Journal: Proc Natl Acad Sci U S A Date: 2010-06-14 Impact factor: 11.205

4. Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.

Authors: Tomoya Sameshima; Ryo Iizuka; Taro Ueno; Junichi Wada; Mutsuko Aoki; Naonobu Shimamoto; Iwao Ohdomari; Takashi Tanii; Takashi Funatsu
Journal: J Biol Chem Date: 2010-05-28 Impact factor: 5.157

5. Cytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strands.

Authors: Susumu Kubota; Hiroshi Kubota; Kazuhiro Nagata
Journal: Proc Natl Acad Sci U S A Date: 2006-05-22 Impact factor: 11.205

Single-molecule observation of protein-protein interactions in the chaperonin system.

1. Single-molecule imaging of cooperative assembly of gamma-hemolysin on erythrocyte membranes.

2. The interaction of beta(2)-glycoprotein I domain V with chaperonin GroEL: the similarity with the domain V and membrane interaction.

3. Single-molecule spectroscopy of protein folding in a chaperonin cage.

4. Single-molecule study on the decay process of the football-shaped GroEL-GroES complex using zero-mode waveguides.

5. Cytosolic chaperonin protects folding intermediates of Gbeta from aggregation by recognizing hydrophobic beta-strands.

6. Fast-scanning atomic force microscopy reveals the ATP/ADP-dependent conformational changes of GroEL.

7. Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES.

Review 8. Single-molecule biophysics: at the interface of biology, physics and chemistry.

Review 9. High-speed AFM and nano-visualization of biomolecular processes.

10. Football- and bullet-shaped GroEL-GroES complexes coexist during the reaction cycle.