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

Callebaut, Isabelle; Mornon, Jean‐Paul

doi:10.1016/0014-5793(95)01109-r

Cited by 82 publications

(70 citation statements)

References 40 publications

(70 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…A certain degree of homology to FKBPs has been reported for the domain of TF encompassing residues 142-241 [12]. Indeed, when TF which is 432 amino acids in length was subjected to digestion by subtilisin, a single remaining active fragment was generated.…”

Section: Discussionmentioning

confidence: 99%

“…Thus, the PPIase domain retains the magnitude of activity usually found for FKBPs. For the amino acid sequence region encompassing the PPIase domain a certain degree of homology with FKBPs was shown [12]. However, in contrast to other FKBPs authentic TF as well as the 11.…”

Section: Enzymatic and Structural Propertiesmentioning

confidence: 99%

“…However, in contrast to other FKBPs authentic TF as well as the 11. [12,38]. The amino acyl residues enclosed to the PPIase active fragment are underlined.…”

Section: Enzymatic and Structural Propertiesmentioning

confidence: 99%

See 2 more Smart Citations

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

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

Section: Enzymatic and Structural Propertiesmentioning

confidence: 99%

See 1 more Smart Citation

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

View full text Add to dashboard Cite

show abstract

“…Trigger factor is the major protein that cross-links to virtually all nascent chains of secretory and cytosolic proteins tested (Valent et al, 1995;Hesterkamp and Bukau, 1996a). Sequence analysis and substrate specificity suggests that trigger factor contains a central domain belonging to the FKBP family (Callebaut and Mornon, 1995;Hesterkamp and Bukau, 1996b). Besides the central PPIase domain, trigger factor has a ribosome binding domain at the N-terminal domain and its C-terminal domain may strengthen the binding (Hesterkamp et al, 1997).…”

mentioning

confidence: 99%

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

2004

View full text Add to dashboard Cite

Immunophilins are defined as receptors for immunosuppressive drugs including cyclosporin A, FK506, and rapamycin. The cyclosporin A receptors are referred to as cyclophilins (CYPs) and FK506-and rapamycin-binding proteins are abbreviated as FKBPs. These two groups of proteins (collectively called immunophilins) share little sequence homology, but both have peptidyl prolyl cis/trans isomerase (PPIase) activity that is involved in protein folding processes. Studies have identified immunophilins in all organisms examined including bacteria, fungi, animals, and plants. Nevertheless, the physiological function of immunophilins is poorly understood in any organism. In this study, we have surveyed the genes encoding immunophilins in Arabidopsis genome. A total of 52 genes have been found to encode putative immunophilins, among which 23 are putative FKBPs and 29 are putative CYPs. This is by far the largest immunophilin family identified in any organism. Both FKBPs and CYPs can be classified into single domain and multiple domain members. The single domain members contain a basic catalytic domain and some of them have signal sequences for targeting to a specific organelle. The multiple domain members contain not only the catalytic domain but also defined modules that are involved in protein-protein interaction or other functions. A striking feature of immunophilins in Arabidopsis is that a large fraction of FKBPs and CYPs are localized in the chloroplast, a possible explanation for why plants have a larger immunophilin family than animals. Parvulins represent another family of PPIases that are unrelated to immunophilins in protein sequences and drug binding properties. Three parvulin genes were found in Arabidopsis genome. The expression of many immunophilin and parvulin genes is ubiquitous except for those encoding chloroplast members that are often detected only in the green tissues. The large number of genes and diversity of structure domains and cellular localization make PPIases a versatile superfamily of proteins that clearly function in many cellular processes in plants.Immunosuppressive drugs cyclosporin A (CsA), FK506, and rapamycin are used clinically in transplantation to prevent graft rejection. During the course to understand the molecular mechanisms of immunosuppression by CsA, FK506, and rapamycin, the cellular receptors of these drugs have been purified and characterized (Schreiber, 1991;Fruman et al., 1994). CsA binds to a family of receptors named cyclophilins (CyPs), and FK506 and rapamycin bind to a distinct set of receptors called FKBPs (FK506 and rapamycin-binding proteins). Cyclophilins and FKBPs are collectively referred to as immunophilins (Schreiber, 1991).The complexes formed by immunophilins and their cognate ligands are the functional modules for immunosuppression. The FKBP12-FK506 and CyPCsA complexes, but not their separate components, bind to and inhibit the activity of calcineurin, a Ca 21 , calmodulin-dependent protein phosphatase (Liu et al., 1991). Studies have demonstrated that inhib...

show abstract

“…Hesterkamp et al and Callebaut and Mornon reported on a homology of trigger factor with PPIases of the FKBP family [10,13]. The region of homology is located within the central part of the trigger factor polypeptide chain, between residues 165 and 240, and is restricted to residues forming the substrate binding pocket in human FKBP12 [14][15][16].…”

Section: Structure-function Relationship Of Trigger Factor's Ppiase Amentioning

confidence: 99%

The Escherichia coli trigger factor

Hesterkamp

Bukau

1996

FEBS Letters

View full text Add to dashboard Cite

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...

show abstract

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

Cited by 82 publications

References 40 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

Immunophilins and Parvulins. Superfamily of Peptidyl Prolyl Isomerases in Arabidopsis

The Escherichia coli trigger factor

Contact Info

Product

Resources

About