Trigger Factor from Thermus thermophilus Is a Zn2+-dependent Chaperone

Suno, Ryoji; Taguchi, Hideki; Masui, R.; Odaka, Masafumi; Yoshida, Masasuke

doi:10.1074/jbc.m311572200

Cited by 12 publications

(22 citation statements)

References 32 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In this position, surrounded on one side by the M domain of the SRP and on the other side by the hydrophobic cleft of the trigger factor, the nascent chain can be monitored by both factors ( Figures 4E and 4F and step B in Figure 5). Such a model is consistent with previous biochemical data suggesting that, instead of promoting protein folding, TF delays it, both upon dilution from denaturant (Suno et al, 2004) as well as during de novo protein synthesis, in vitro and in vivo (Agashe et al, 2004).…”

Section: Discussionsupporting

confidence: 92%

The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction

et al. 2005

View full text Add to dashboard Cite

This study presents the X-ray structure of the N-terminal binding domain of the D. radiodurans trigger factor (TF) in complex with the D. radiodurans large ribosomal subunit. At 3.35 A, a complete description of the interactions with ribosomal proteins L23, L29, and 23S rRNA are disclosed, many of which differ from those found previously for a heterologous bacterial-archaeal TF-ribosome complex. The beta hairpin loop of eubacterial L24, which is shorter in archaeal ribosomes, contacts the TF and severely diminishes the molecular cradle proposed to exist between the TF and ribosome. Bound to the ribosome, TF exposes a hydrophobic crevice large enough to accommodate the nascent polypeptide chain. Superimposition of the full-length TF and the signal-recognition particle (SRP) onto the complex shows that simultaneous cohabitation is possible, in agreement with biochemical data, and suggests a model for the interplay of TF, SRP, and the nascent chain during translation.

show abstract

Section: Discussionsupporting

confidence: 92%

The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction

et al. 2005

View full text Add to dashboard Cite

show abstract

“…Thermus thermophilus (15), Hsp70 and Hsp100 chaperones (16) and the chaperonins (17). Here, we describe investigation of the folding of guanidine-denatured GFPuv in the presence and absence of Escherichia coli TF.…”

mentioning

confidence: 99%

Trigger Factor Assisted Folding of Green Fluorescent Protein

Xie

Zhou

2007

Biochemistry

View full text Add to dashboard Cite

Guanidine induced equilibrium and kinetic folding of a variant of green fluorescent protein (F99S/M153T/V163A, GFPuv) was studied. Using manual mixing and stopped-flow techniques, we combined different probes, including tryptophan fluorescence, chromophore fluorescence and reactivity with DTNB, to trace the spontaneous and TF-assisted folding of guanidine denatured GFPuv. We found that both unfolding and refolding of GFPuv occurred in a stepwise manner and a stable intermediate was populated under equilibrium conditions. The thermodynamic parameters obtained show that the intermediate state of GFPuv is quite compact compared to the denatured state and most of the green fluorescence is retained in this state. By studying GFPuv folding assisted by TF and a number of TF mutants, we found that wild-type TF catalyzes proline isomerization and accelerates the folding rate at low TF concentrations, but retards GFPuv folding and decelerates the folding rate at high TF concentrations. This reflects the two activities of TF, as an enzyme and as a chaperone. A general mechanism of TF assisted protein folding is discussed.

show abstract

“…GroEL and trigger factor represent two out of the four intracellular molecular chaperones in E. coli (Houry 2001). Trigger factor has been reported to be regulated by Cd(II) stress (Ferianc et al 1998), and a homolog in Thermus thermophilus (Suno et al 2004) has recently been reported to bind Zn(II). Lastly, the most abundant protein in E. coli, TufB (Weijland et al 1992), was upregulated along with the ribosomal protein L9 (Herbst et al 1994) and carbamoyl phosphate synthase (CarB) (Rubino et al 1987).…”

Section: D Gels Of E Coli Culturesmentioning

confidence: 99%

Probing the adaptive response of Escherichia coli to extracellular Zn(II)

et al. 2006

View full text Add to dashboard Cite

The adaptive response of Escherichia coli cells to differing intracellular and extracellular Zn(II) concentrations was evaluated by two-dimensional gel electrophoresis and peptide identifications. Twenty-one Zn(II)-responsive proteins, which were previously not known to be associated with Zn(II), were identified. Most of the proteins were related to cellular metabolism and include membrane transporters and glycolytic and TCA-associated enzymes. The expression levels of no known Zn(II) transporters were identified with these studies. The results of these studies suggest a role of Zn(II) in the expression levels of several E. coli proteins, and the results are discussed in light of recent genomic profiling studies on the adaptive response of E. coli cells to stress by Zn(II) excess.

show abstract

Trigger Factor from Thermus thermophilus Is a Zn2+-dependent Chaperone

Cited by 12 publications

References 32 publications

The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction

The Binding Mode of the Trigger Factor on the Ribosome: Implications for Protein Folding and SRP Interaction

Trigger Factor Assisted Folding of Green Fluorescent Protein

Probing the adaptive response of Escherichia coli to extracellular Zn(II)

Contact Info

Product

Resources

About