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Gene Review

tig  -  trigger factor

Escherichia coli O157:H7 str. Sakai

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Disease relevance of tig

  • While dnaK and tig are the essential components for nascent polypeptide folding in E. coli, deletion did not confer synthetic lethality in B. subtilis, suggesting that under normal growth conditions, another system or mechanism with a specific role prevails [1].
  • Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone [2].
  • We identified a gene, designated tig, encoding a protein homologous to trigger factor (TF), a cytosolic ribosome-associated chaperone, in the genome of Listeria monocytogenes [3].
  • A Homolog of Bacillus subtilis Trigger Factor in Listeria monocytogenes Is Involved in Stress Tolerance and Bacterial Virulence [3].
  • X-ray crystallography and chemical cross-linking were used to study the roles of the N- and C-terminal domains of Thermotoga maritima TF in TF oligomerization and chaperone activity [4].

High impact information on tig

  • L23 is essential for the growth of E. coli and the association of Trigger Factor with the ribosome, whereas L29 is dispensable in both processes [5].
  • TF was originally proposed to function in protein translocation across membranes but altering cellular content of TF did not affect this process in vivo [6].
  • Here, we show that the secretion-dedicated chaperone SecB efficiently suppresses both the temperature sensitivity and the aggregation-prone phenotypes of a strain lacking both TF and DnaK [7].
  • The features of this groove complement well the determined substrate specificity of TF [8].
  • Trigger factor (TF) is the first protein-folding chaperone to interact with a nascent peptide chain as it emerges from the ribosome [9].

Biological context of tig

  • Based on our results, we propose that TF and DnaK promote protein folding by distinct (but complementary) mechanisms [10].
  • Trigger factor has a binding site on ribosomes, which is a prerequisite for its efficient association with nascent chains and its proposed function as a cotranslational folding catalyst [11].
  • In vivo, the loss of TF is compensated by the induction of the heat shock response and thus enhanced levels of DnaK [12].
  • However, in vivo it showed a reduced capacity to persist in the spleens and livers of infected mice, revealing that TF has a role in the pathogenicity of L. monocytogenes [3].
  • The nucleotide sequence encoding the amino acid residues Met-140 to Ala-250 of the TF was cloned into vector pQE32 [13].

Anatomical context of tig


Associations of tig with chemical compounds

  • Mutation of an exposed glutamate in L23 prevents Trigger Factor from interacting with ribosomes and nascent chains, and causes protein aggregation and conditional lethality in cells that lack the protein repair function of the DnaK chaperone [5].
  • TF F198A retained a similar binding specificity toward membrane-bound peptides, assisted the refolding of denatured d-glyceraldehyde-3-phosphate dehydrogenase in vitro, and associated with nascent polypeptides in an in vitro transcription/translation system [14].
  • Unexpectedly, EDTA completely abolished the folding-arrest activity of TF, and analysis revealed that the TF from our preparation contained approximately 0.5 mol Zn2+/mol TF [2].

Analytical, diagnostic and therapeutic context of tig

  • Upon ATP addition, GroEL and TF dissociated together from CRAG but remained tightly associated with each other even upon gel filtration [6].


  1. DnaK chaperone machine and trigger factor are only partially required for normal growth of Bacillus subtilis. Reyes, D.Y., Yoshikawa, H. Biosci. Biotechnol. Biochem. (2002) [Pubmed]
  2. Trigger factor from Thermus thermophilus is a Zn2+-dependent chaperone. Suno, R., Taguchi, H., Masui, R., Odaka, M., Yoshida, M. J. Biol. Chem. (2004) [Pubmed]
  3. A Homolog of Bacillus subtilis Trigger Factor in Listeria monocytogenes Is Involved in Stress Tolerance and Bacterial Virulence. Bigot, A., Botton, E., Dubail, I., Charbit, A. Appl. Environ. Microbiol. (2006) [Pubmed]
  4. Structures of and interactions between domains of trigger factor from Thermotoga maritima. Martinez-Hackert, E., Hendrickson, W.A. Acta Crystallogr. D Biol. Crystallogr. (2007) [Pubmed]
  5. L23 protein functions as a chaperone docking site on the ribosome. Kramer, G., Rauch, T., Rist, W., Vorderwülbecke, S., Patzelt, H., Schulze-Specking, A., Ban, N., Deuerling, E., Bukau, B. Nature (2002) [Pubmed]
  6. Trigger factor is involved in GroEL-dependent protein degradation in Escherichia coli and promotes binding of GroEL to unfolded proteins. Kandror, O., Sherman, M., Rhode, M., Goldberg, A.L. EMBO J. (1995) [Pubmed]
  7. SecB is a bona fide generalized chaperone in Escherichia coli. Ullers, R.S., Luirink, J., Harms, N., Schwager, F., Georgopoulos, C., Genevaux, P. Proc. Natl. Acad. Sci. U.S.A. (2004) [Pubmed]
  8. Binding specificity of Escherichia coli trigger factor. Patzelt, H., Rüdiger, S., Brehmer, D., Kramer, G., Vorderwülbecke, S., Schaffitzel, E., Waitz, A., Hesterkamp, T., Dong, L., Schneider-Mergener, J., Bukau, B., Deuerling, E. Proc. Natl. Acad. Sci. U.S.A. (2001) [Pubmed]
  9. Trigger factor binding to ribosomes with nascent Peptide chains of varying lengths and sequences. Raine, A., Lovmar, M., Wikberg, J., Ehrenberg, M. J. Biol. Chem. (2006) [Pubmed]
  10. Trigger factor retards protein export in Escherichia coli. Lee, H.C., Bernstein, H.D. J. Biol. Chem. (2002) [Pubmed]
  11. The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes. Hesterkamp, T., Deuerling, E., Bukau, B. J. Biol. Chem. (1997) [Pubmed]
  12. Trigger Factor and DnaK possess overlapping substrate pools and binding specificities. Deuerling, E., Patzelt, H., Vorderwülbecke, S., Rauch, T., Kramer, G., Schaffitzel, E., Mogk, A., Schulze-Specking, A., Langen, H., Bukau, B. Mol. Microbiol. (2003) [Pubmed]
  13. An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity. Stoller, G., Tradler, T., Rücknagel, K.P., Rahfeld J-U, n.u.l.l., Fischer, G. FEBS Lett. (1996) [Pubmed]
  14. Trigger factor peptidyl-prolyl cis/trans isomerase activity is not essential for the folding of cytosolic proteins in Escherichia coli. Kramer, G., Patzelt, H., Rauch, T., Kurz, T.A., Vorderwülbecke, S., Bukau, B., Deuerling, E. J. Biol. Chem. (2004) [Pubmed]
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