Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

Hesterkamp, Thomas; Hauser, Stefanie; Lütcke, Henrich; Bukau, Bernd

doi:10.1073/pnas.93.9.4437

Cited by 230 publications

(180 citation statements)

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“…Much of our current understanding about the functions and mechanism of this class of chaperones is based on the studies done with TF. TF is a 48 kDa protein that binds to ribosomes in a 1:1 stoichiometry and interacts with nascent chains in an ATP independent manner (Hesterkamp et al, 1996). Recognition of ribosome bound polypeptide by TF is mediated by short sequences enriched in hydrophobic (particularly aromatic) residues (Patzelt et al, 2001).…”

Section: Figure 2: the Major Components Of The Proteostasis Network (mentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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Section: Figure 2: the Major Components Of The Proteostasis Network (mentioning

confidence: 99%

Firefly luciferase mutants as sensors of proteome stress

et al. 2011

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“…Rather, a major cotranslational interaction has been identified recently with a component known as trigger factor, which has peptidyl prolyl isomerase activity (Stoller et al, 1995;Valent et al, 1995;Hesterkamp et al, 1996). GroEL thus appears to function posttranslationally, binding to polypeptide chains that have been released from the translation machinery or from other components, perhaps including Hsp70 proteins.…”

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confidence: 99%

GroEL‐Mediated protein folding

1997

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I. Architecture of GroEL and GroES and the reaction pathwayA. Architecture of the chaperonins B. Reaction pathway of GroEL-GroES-mediated folding 3. 4. 5.Role of hydrophobicity in recognition Homologous proteins with differing recognition-differences in primary structure versus effects on folding Concluding remarksKeywords: chaperonin; GroES; Hsp60; kinetic partitioning; mechanism of action; X-ray structureThe early studies of Anfinsen and co-workers established that the 1973). Under physiologic conditions inside the cell, however, the primary structure of a protein contains all the information necesfolding process for many proteins, particularly those with multisary to direct the native secondary and tertiary fold (Anfinsen, domain structures, is prone to producing a variety of misfolded species and aggregates. Recent studies indicate that a specialized

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“…Searching for E. coli proteins associated with nascent polypeptide chains of 13-galactosidase in an in vitro transcriptiontranslation system, Bukau and coworkers observed a salt-resistant association of trigger factor with translating ribosomes [10]. This association was sensitive to puromycin treatment and thus dependent on the presence of nascent 13-galactosidase.…”

Section: Trigger Factor Associates With Nascent Polypeptide Chains Anmentioning

confidence: 99%

“…PII S00 1 4-5793(96)00582-0 and demonstrated PPIase activity for purified trigger factor. Together, a role for trigger factor as a co-translationally acting folding catalyst was proposed [10].…”

Section: Trigger Factor Associates With Nascent Polypeptide Chains Anmentioning

confidence: 99%

“…P48 and trigger factor competed for crosslinking to prePhoE suggesting overlapping substrate specificities of both proteins. In contrast to P48, however, trigger factor was also efficiently crosslinked to non-secretory nascent chains [9].Searching for E. coli proteins associated with nascent polypeptide chains of 13-galactosidase in an in vitro transcriptiontranslation system, Bukau and coworkers observed a salt-resistant association of trigger factor with translating ribosomes [10]. This association was sensitive to puromycin treatment and thus dependent on the presence of nascent 13-galactosidase.…”

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The Escherichia coli trigger factor

Hesterkamp

Bukau

1996

FEBS Letters

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E. coli trigger factor is an abundant cytosolic protein originally identified by its ability to maintain the precursor of a secretory protein in a translocation competent form. Recent studies shed new light on the function of this protein. Trigger factor was found to be a peptidyl-prolyl-cisltrans-isomerase capable of catalysing protein folding in vitro, to associate with nascent cytosolic and secretory polypeptide chains, and to cooperate with the GroEL chaperone in promoting proteolysis of an unstable polypeptide in vivo. These findings suggest roles for trigger factor in various folding processes of secretory as well as cytosolic proteins.Key words: Ribosome; Prolyl isomerase; Chaperone; Protein folding; Translocation; Proteolysis DiscoveryTrigger factor was discovered in a biochemical screen for cytosolic components of the secretion machinery of E. coli. Analysing the translocation of the outer membrane protein A (OmpA) across inner membrane vesicles in vitro, Wickner and coworkers identified an activity that stabilized the precursor (proOmpA) in a loosely folded conformation thereby stimulating its membrane translocation. This activity was shown to reside in a monomeric protein with an apparent molecular weight of 60 kDa, termed trigger factor [1 3]. Trigger factor formed stable 1:1 complexes with chemically denatured proOmpA that was diluted from denaturant. When proOmpA was allowed to fold in the absence of trigger factor, however, translocation of proOmpA could not be restored, indicating that trigger factor could not actively unfold the substrate [2]. Genetic analysisThe tig gene encoding trigger factor was cloned [4] and its expression found to be growth phase controlled and thus coregulated with genes encoding ribosomal components (F. Neidhardt, personal communication cited in [4]). Genetic analysis of the in vivo function of trigger factor using a conditional depletion strain failed to provide new insights. At conditions depleting trigger factor to less than 5% of the normal levels, cells remain fully viable but form filaments indicative of cell division defects. No defects in the translocation of proOmpA, even in a trigger factor depletion strain with an additional deficiency for the secretion specific SecB chaperone, were observed [4]. These results suggest that trigger factor is dispensable for growth of E. coli, although analysis of a rig *Corresponding author. Fax: (49) (6221) 545892. E-mail: bukau@sun0.urz.uni-heidelberg.de knockout mutant is required for a proof. It is not excluded either that trigger factor does play an important role in metabolism but that backup systems exist replacing missing trigger factor functions under depletion conditions. An important physiological role of trigger factor is indicated by the finding that tig homologs exist in other bacterial genomes [5][6][7] including that of Mycoplasma genitalium which is believed to contain the minimum set of genes required for life [7]. Trigger factor associates with nascent polypeptide chains and has prolyl isomerase ac...

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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

Abstract: Correct folding of newly synthesized proteins is proposed to be assisted by molecular chaperones and folding catalysts. To

Cited by 230 publications

References 23 publications

Firefly luciferase mutants as sensors of proteome stress

Firefly luciferase mutants as sensors of proteome stress

GroEL‐Mediated protein folding

The Escherichia coli trigger factor

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