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Literature DB >> 31371450

Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes.

Abstract

The chaperonin GroEL and its co-chaperonin GroES form both GroEL-GroES bullet-shaped and GroEL-GroES2 football-shaped complexes. The residence time of protein substrates in the cavities of these complexes is about 10 and 1 s, respectively. There has been much controversy regarding which of these complexes is the main functional form. Here, we show using computational analysis that GroEL protein substrates have a bimodal distribution of folding times, which matches these residence times, thereby suggesting that both bullet-shaped and football-shaped complexes are functional. More generally, co-existing complexes with different stoichiometries are not mutually exclusive with respect to having a functional role and can complement each other.

Entities: Gene

Keywords: GroEL; PSIPRED; bioinformatics; chaperonin; kinetics; molecular machines; protein folding

Mesh：

Substances：

Year: 2019 PMID： 31371450 PMCID： PMC6746456 DOI： 10.1074/jbc.AC119.010299

Source DB: PubMed Journal: J Biol Chem ISSN： 0021-9258 Impact factor: 5.157

29 in total

1. Protein secondary structure prediction based on position-specific scoring matrices.

Authors: D T Jones
Journal: J Mol Biol Date: 1999-09-17 Impact factor: 5.469

2. Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.

Authors: Dmitry N Ivankov; Alexei V Finkelstein
Journal: Proc Natl Acad Sci U S A Date: 2004-06-07 Impact factor: 11.205

3. ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

Authors: H R Saibil; D Zheng; A M Roseman; A S Hunter; G M Watson; S Chen; A Auf Der Mauer; B P O'Hara; S P Wood; N H Mann; L K Barnett; R J Ellis
Journal: Curr Biol Date: 1993-05-01 Impact factor: 10.834

Review 4. What distinguishes GroEL substrates from other Escherichia coli proteins?

Authors: Ariel Azia; Ron Unger; Amnon Horovitz
Journal: FEBS J Date: 2012-01-04 Impact factor: 5.542

5. Protein folding in the cell: an inside story.

Authors: Arthur L Horwich
Journal: Nat Med Date: 2011-10-11 Impact factor: 53.440

6. A systematic survey of in vivo obligate chaperonin-dependent substrates.

Authors: Kei Fujiwara; Yasushi Ishihama; Kenji Nakahigashi; Tomoyoshi Soga; Hideki Taguchi
Journal: EMBO J Date: 2010-04-01 Impact factor: 11.598

7. Image analysis by electron microscopy of two-dimensional crystals developed on a mercury surface of chaperonin from Thermus thermophilus.

Authors: N Ishii; H Taguchi; M Yoshida; H Yoshimura; K Nagayama
Journal: J Biochem Date: 1991-12 Impact factor: 3.387

Reconciling the controversy regarding the functional importance of bullet- and football-shaped GroE complexes.

1. Protein secondary structure prediction based on position-specific scoring matrices.

2. Prediction of protein folding rates from the amino acid sequence-predicted secondary structure.

3. ATP induces large quaternary rearrangements in a cage-like chaperonin structure.

Review 4. What distinguishes GroEL substrates from other Escherichia coli proteins?

5. Protein folding in the cell: an inside story.

6. A systematic survey of in vivo obligate chaperonin-dependent substrates.

7. Image analysis by electron microscopy of two-dimensional crystals developed on a mercury surface of chaperonin from Thermus thermophilus.

8. Symmetric GroEL:GroES2 complexes are the protein-folding functional form of the chaperonin nanomachine.

9. Substrate protein switches GroE chaperonins from asymmetric to symmetric cycling by catalyzing nucleotide exchange.

10. Proteome-wide analysis of chaperonin-dependent protein folding in Escherichia coli.

1. Chloroplast Chaperonin-Mediated Targeting of a Thylakoid Membrane Protein.

2. Temperature Regulates Stability, Ligand Binding (Mg²⁺ and ATP), and Stoichiometry of GroEL-GroES Complexes.

3. Structural basis for active single and double ring complexes in human mitochondrial Hsp60-Hsp10 chaperonin.

4. Slowdown of Water Dynamics from the Top to the Bottom of the GroEL Cavity.