The gene for Campylobacter trigger factor: evidence for multiple transcription start sites and protein products

Griffiths, P.L.; Park, Robert W. A.; Connerton, Ian F.

doi:10.1099/13500872-141-6-1359

Cited by 13 publications

(12 citation statements)

References 41 publications

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“…5), substitution through Val revealed a substantial increase in the Ki value from 0.6 nM to 350 nM [27]. In contrast to other FKBPs the TF of E. coli and the recently described TF of Campylobacter jejuni [28] contain a glutamate residue at this position. For the TF of C. jejuni, however, data about PPIase activity and possibly FK506 binding have not been available until now.…”

Section: Discussionmentioning

confidence: 80%

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

Stoller¹,

Tradler²,

Rücknagel³

et al. 1996

FEBS Letters

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The 48 kDa trigger factor (TF) of E. coli was shown to be a peptidyl-prolyl cisltrans isomerase (PPIase). Its location on a ribosomal particle is unique among the PPIases described so far, and suggests a role in de novo protein folding. The trigger factor was investigated with regard to a domain carrying the catalytic activity. An enzymatieally active fragment could be isolated after proteolysis by subtifisin. The resulting polypeptide was analysed by N-terminal sequencing and MALDI-TOF mass spectrometry revealing an 11.8 kDa fragment of TF encompassing the amino acid residues Arg-145 to Glu-251. The nucleotide sequence encoding the amino acid residues Met-140 to Ala-250 of the TF was cloned into vector pQE32. After expression in E. coli the resulting His-tagged polypeptide was isolated on an Ni 2+-NTA column. Subsequent digestion with subtifisin and anionexchange chromatography yielded a TF fragment encompassing amino acids Gin-148 to Thr-249. This fragment may represent the catalytic core of TF since PPIase activity with a specificity constant kcat/Km of 1.3 ~1-1 s -l could be demonstrated when using Suc-Ala-Phe-Pro-Phe-NH-Np as a substrate. Moreover, as was observed for the complete, authentic TF the PPIase activity of the fragment was not inhibited by the peptidomacrofide FK506.

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Section: Discussionmentioning

confidence: 80%

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

Stoller¹,

Tradler²,

Rücknagel³

et al. 1996

FEBS Letters

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“…All the regular secondary structures' of the FKBP Jold are also found in the trigger factor sequence Similarities in cluster shape, distribution and size between trigger factor and FKBPs are identified all along the HCA plots ( References can be found in [1] and in [8,9] (slyD); [10,11] (yeast FPR3, FKBP-47); [12] (Spodopterafrugiperda FKBP46); [13] (FKBP-33); [14] (Escherichia coli and Pseudomonas fluorescens FKBX); ( [15,16] and this study) (Escherichia coli and Campylobacter jujuni trigger factor).…”

Section: Resultsmentioning

confidence: 99%

“…Bold and underlined letters indicate mismatches. [32], ncFKBP-12, Neurospora crassa FKBP-12 [33]; scFKBP-12, Saccharomyces cerevisiae FKBP-12 [34]; hHBI, human Hsp90-binding immunophilin (also known as FKBP52 or p59) [35]; ctMIE Chlamydia trachomatis MIP [36]; ecFKBY, Escherichia coil probable FKBP-type 22kD ppiase -ytec-(swissprot identifier: fkby_ecoli): ecTIG, Escherichia coli trigger factor [16]; cjTIG, Campylobacterjujuni trigger factor [15].…”

Section: Ip G Fedg I Kg H Ka G Eeft I Dvt__f Pe__e Y -H Cjujuni Tig mentioning

confidence: 99%

Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family

Callebaut

Mornon

1995

FEBS Letters

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“…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].…”

Section: Genetic Analysismentioning

confidence: 99%

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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The gene for Campylobacter trigger factor: evidence for multiple transcription start sites and protein products

Cited by 13 publications

References 41 publications

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl‐prolyl cis/trans isomerase activity

Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family

The Escherichia coli trigger factor

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