Chaperone and antichaperone activities of trigger factor

Huang, Guo-Chang; Chen, Jiajia; Liu, Chuan-Peng; Zhou, Jun‐Mei

doi:10.1046/j.1432-1033.2002.03145.x

Cited by 19 publications

(15 citation statements)

References 31 publications

(45 reference statements)

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“…To determine the contribution of individual FKBP26 domains to chaperone activity, we tested the different constructs in a well established in vitro chaperone assay using denatured hen egg white lysozyme as a substrate 23,24 Chemically denatured lysozyme aggregated rapidly upon 100-fold dilution, but stoichiometric amounts of FKBP26 efficiently prevented lysozyme aggregation, as no light-scattering signal at 360 nm was observed (Fig. 1b).…”

Section: Resultsmentioning

confidence: 99%

Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

Martı́nez-Hackert

Hendrickson

2011

Journal of Molecular Biology

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Summary In the cell, protein folding is mediated by folding catalysts and chaperones. The two functions are often linked, especially when the catalytic module forms part of a multidomain protein, as in Methanococcus jannaschii peptidyl-prolyl cis/trans isomerase (PPIase) FKBP26. Here we show that FKBP26 chaperone activity requires both a 50-residue insertion in the catalytic FKBP domain, also called ‘Insert-in-Flap’ or IF domain, and also an 80-residue C-terminal domain. We determined FKBP26 structures from four crystal forms and analyzed chaperone domains in light of their ability to mediate protein-protein interactions. FKBP26 is a crescent-shaped homodimer. We reason that folding proteins are bound inside the large crescent cleft, thus enabling their access to inward-facing PPIase catalytic sites and ipsilateral chaperone domain surfaces. As these chaperone surfaces participate extensively in crystal lattice contacts, we speculate that the observed lattice contacts reflect a proclivity for protein associations and represent substrate interactions by FKBP26 chaperone domains. Finally, we find that FKBP26 is an exceptionally flexible molecule, suggesting a mechanism for non-specific substrate recognition.

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Section: Resultsmentioning

confidence: 99%

Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

Martı́nez-Hackert

Hendrickson

2011

Journal of Molecular Biology

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“…The higher the concentration of TF, the greater the chance of recapture of substrate intermediates by TF. It was suggested that this binding effect can lead to the arrest of folding (Huang et al, 2002, 2000), so that GFPuv folding was no longer limited by proline isomerization. Thus, it can be concluded that though the limiting-rate role of all the proline residues together in FPs is demonstrated, the role played by each of them is the task of future investigations.…”

Section: Unfolding–refolding Of Fluorescent Proteinsmentioning

confidence: 99%

Beta-Barrel Scaffold of Fluorescent Proteins

Stepanenko

Kuznetsova

Verkhusha

et al. 2013

International Review of Cell and Molecular Biology

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This review focuses on the current view of the interaction between the β-barrel scaffold of fluorescent proteins and their unique chromophore located in the internal helix. The chromophore originates from the polypeptide chain and its properties are influenced by the surrounding protein matrix of the β-barrel. On the other hand, it appears that a chromophore tightens the β-barrel scaffold and plays a crucial role in its stability. Furthermore, the presence of a mature chromophore causes hysteresis of protein unfolding and refolding. We survey studies measuring protein unfolding and refolding using traditional methods as well as new approaches, such as mechanical unfolding and reassembly of truncated fluorescent proteins. We also analyze models of fluorescent protein unfolding and refolding obtained through different approaches, and compare the results of protein folding in vitro to co-translational folding of a newly synthesized polypeptide chain.

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“…The high cytosolic concentration of TF has recently been linked to a distinct functional role of the chaperone in maintaining newly translated polypeptides in a folding-competent state in the E. coli cytoplasm (35). A distinct antichaperone activity has also been described for TF, however, whereby substoichiometric concentrations of TF lead to increased polypeptide aggregation, whereas high TF/polypeptide ratios can also delay folding as the chaperone maintains polypeptides in a non-native state without promoting their complete refolding (9).…”

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confidence: 99%

Trigger Factor from the Psychrophilic Bacterium Psychrobacter frigidicola Is a Monomeric Chaperone

et al. 2009

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In eubacteria, trigger factor (TF) is the first chaperone to interact with newly synthesized polypeptides and assist their folding as they emerge from the ribosome. We report the first characterization of a TF from a psychrophilic organism. TF from Psychrobacter frigidicola (TF Pf ) was cloned, produced in Escherichia coli, and purified. Strikingly, cross-linking and fluorescence anisotropy analyses revealed it to exist in solution as a monomer, unlike the well-characterized, dimeric E. coli TF (TF Ec ). Moreover, TF Pf did not exhibit the downturn in reactivation of unfolded GAPDH (glyceraldehyde-3-phosphate dehydrogenase) that is observed with its E. coli counterpart, even at high TF/GAPDH molar ratios and revealed dramatically reduced retardation of membrane translocation by a model recombinant protein compared to the E. coli chaperone. TF Pf was also significantly more effective than TF Ec at increasing the yield of soluble and functional recombinant protein in a cell-free protein synthesis system, indicating that it is not dependent on downstream systems for its chaperoning activity. We propose that TF Pf differs from TF Ec in its quaternary structure and chaperone activity, and we discuss the potential significance of these differences in its native environment.The folding of cytosolic proteins is coordinated by three chaperone systems in eubacteria: trigger factor (TF), DnaK and its cofactors DnaJ and GrpE, and GroEL, together with its cofactor GroES. As TF alone interacts with the ribosomes, it is the first chaperone to bind newly synthesized polypeptides and assist their folding, whereupon it passes them to downstream chaperone systems (12). It has recently been shown that, for multidomain proteins, TF and the DnaK system cooperate to slow down folding and cause a shift to a posttranslational folding mode (24). TF also plays an important role in the regulation of protein translocation due to its position at the ribosome exit tunnel (1, 24).TF is highly abundant in E. coli (up to 40 M), with most TF molecules existing in an equilibrium between its monomeric and dimeric states in the cytosol (28). The high cytosolic concentration of TF has recently been linked to a distinct functional role of the chaperone in maintaining newly translated polypeptides in a folding-competent state in the E. coli cytoplasm (35). A distinct antichaperone activity has also been described for TF, however, whereby substoichiometric concentrations of TF lead to increased polypeptide aggregation, whereas high TF/polypeptide ratios can also delay folding as the chaperone maintains polypeptides in a non-native state without promoting their complete refolding (9).E. coli TF (TF Ec ) is composed of an N-terminal ribosomebinding tail (domain I), an internal domain with peptidyl-prolyl cis/trans isomerase (PPIase) activity (domain II), and a Cterminal domain III that is involved in its chaperone activity (26). The importance of the PPIase domain remains unclear as TF binds non-native nascent polypeptides lacking proline residues (29), w...

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Chaperone and antichaperone activities of trigger factor

Cited by 19 publications

References 31 publications

Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

Structural Analysis of Protein Folding by the Long-Chain Archaeal Chaperone FKBP26

Beta-Barrel Scaffold of Fluorescent Proteins

Trigger Factor from the Psychrophilic Bacterium Psychrobacter frigidicola Is a Monomeric Chaperone

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