U.S. flag

An official website of the United States government

Format

Send to:

Choose Destination

Links from GEO Profiles

    • Showing Current items.

    tig trigger factor [ Escherichia coli str. K-12 substr. MG1655 ]

    Gene ID: 945081, updated on 3-Dec-2024

    Summary

    Go to the top of the page Help
    Official Symbol
    tig
    Official Full Name
    trigger factor
    Primary source
    ECOCYC:EG11003
    Locus tag
    b0436
    See related
    ASAP:ABE-0001511
    Gene type
    protein coding
    RefSeq status
    PROVISIONAL
    Organism
    Escherichia coli str. K-12 substr. MG1655 (strain: K-12, substrain: MG1655)
    Lineage
    Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; Enterobacteriaceae; Escherichia
    Also known as
    ECK0430
    Summary
    dnaK and tig mutants are synthetic lethal at 30 degrees C, however, no lethal effects are observed at 23 degrees C. [More information is available at EcoGene: EG11003]. In Escherichia coli Trigger Factor (TF), the tig gene product, is one of three major (along with DnaK and GroEL) chaperones which cooperate in the folding of newly synthesized cytosolic proteins. . [More information is available at EcoCyc: EG11003].
    NEW
    Try the new Gene table
    Try the new Transcript table

    Genomic context

    Go to the top of the page Help
    Sequence:
    NC_000913.3 (455133..456431)

    NC_000913.3Genomic Context describing neighboring genes Neighboring gene putative lipoprotein YajG Neighboring gene DNA-binding transcriptional dual regulator BolA Neighboring gene ATP-dependent Clp protease proteolytic subunit Neighboring gene ATP-dependent Clp protease ATP-binding subunit ClpX

    Genomic regions, transcripts, and products

    Go to the top of the page Help
    Genomic Sequence:
    NC_000913.3

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

    Go to the top of the pageHelp

    Related articles in PubMed

    1. 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, et al. J Biol Chem, 1997 Aug 29. PMID 9268318
    2. Identification of nascent chain interaction sites on trigger factor. Lakshmipathy SK, et al. J Biol Chem, 2007 Apr 20. PMID 17296610
    3. Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family. Callebaut I, et al. FEBS Lett, 1995 Oct 30. PMID 7589537
    4. 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, et al. FEBS Lett, 1996 Apr 15. PMID 8612805
    5. Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains. Hesterkamp T, et al. Proc Natl Acad Sci U S A, 1996 Apr 30. PMID 8633085, Free PMC Article

    See all (107) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Structural insights into the interplay of protein biogenesis factors with the 70S ribosome.
      Title: Structural insights into the interplay of protein biogenesis factors with the 70S ribosome.
    2. Herein we report a study on the mechanism through which TF( A ribosome-associated molecular chaperone trigger factor) recognizes the proline residue in the unfolded client protein during the cis/trans isomerization process
      Title: Structural insight into proline cis/trans isomerization of unfolded proteins catalyzed by the trigger factor chaperone.
    3. by combining the transcriptome and phenotype results, a physiological mechanism underlying the impact of TF deletion on the transcriptome profile was proposed.
      Title: Global Analysis of the Impact of Deleting Trigger Factor on the Transcriptome Profile of Escherichia coli.
    4. The structures reveal distinct degrees of flexibility for the different trigger factor domains, a conformational rearrangement of the N-terminal ribosome-binding domain upon ribosome binding, and an increase in rigidity within trigger factor when the nascent peptide chain is extended.
      Title: Dynamic Behavior of Trigger Factor on the Ribosome.
    5. Trigger factor prevents signal recognition particle binding to the majority of ribosomes, except those presenting SRP-specific signal sequences.
      Title: Interplay between trigger factor and other protein biogenesis factors on the ribosome.
    6. Fused the ANTXR2 ectodomain to the C-terminus of bacterial Trigger Factor (TF), and the fusion protein was overly expressed as a dominant soluble protein in E coli.
      Title: Expression and purification of the functional ectodomain of human anthrax toxin receptor 2 in Escherichia coli Origami B cells with assistance of bacterial Trigger Factor.
    7. Disruption of the TF/DnaK chaperone pathway is rescued by overexpression of the redox-regulated chaperone Hsp33.
      Title: Hsp33 controls elongation factor-Tu stability and allows Escherichia coli growth in the absence of the major DnaK and trigger factor chaperones.
    8. ribosome- and Trigger Factor-specific activities together constitute an efficient mechanism to prevent or even revert premature folding, effectively limiting misfolded intermediates during protein synthesis
      Title: Concerted action of the ribosome and the associated chaperone trigger factor confines nascent polypeptide folding.
    9. Studies of the Escherichia coli chaperone trigger factor (TF) reveal that, though TF can interact with many polypeptides, beta-barrel outer-membrane proteins are the most prominent substrates
      Title: Selective ribosome profiling reveals the cotranslational chaperone action of trigger factor in vivo.
    10. mutant TF lacking the PPIase domain is more efficient than wild-type TF in enhancing the folding yield of multi-domain proteins such as firefly luciferase
      Title: Trigger factor lacking the PPIase domain can enhance the folding of eukaryotic multi-domain proteins in Escherichia coli.
    Submit: New GeneRIF Correction See all GeneRIFs (22)

    Interactions

    Go to the top of the page Help
    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

    Go to the top of the page Help

    Homology

    Gene Ontology Provided by EcoCyc

    Function Evidence Code Pubs
    enables RNA polymerase II CTD heptapeptide repeat P3 isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables RNA polymerase II CTD heptapeptide repeat P6 isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables identical protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables peptidyl-prolyl cis-trans isomerase activity IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables peptidyl-prolyl cis-trans isomerase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables protein binding IPI
    Inferred from Physical Interaction
    more info
    		 PubMed 
    enables protein folding chaperone IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables protein folding chaperone IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ribosome binding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables ribosome binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables ribosome binding IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in 'de novo' cotranslational protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within 'de novo' cotranslational protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in cell division IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within chaperone-mediated protein folding EXP
    Inferred from Experiment
    more info
    		 PubMed 
    involved_in chaperone-mediated protein folding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within chaperone-mediated protein folding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in protein folding IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein transport IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in protein unfolding IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    acts_upstream_of_or_within protein unfolding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of transcription by RNA polymerase II IEA
    Inferred from Electronic Annotation
    more info
    		  
    acts_upstream_of_or_within response to heat IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in stress response to copper ion IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytosol HDA PubMed 
    located_in cytosol IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in membrane HDA PubMed 

    General protein information

    Go to the top of the page Help
    Preferred Names
    trigger factor
    NP_414970.1

    NCBI Reference Sequences (RefSeq)

    Go to the top of the page Help

    NEW Try the new Transcript table

    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_000913.3 Reference assembly

      Range
      455133..456431
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NP_414970.1 trigger factor [Escherichia coli str. K-12 substr. MG1655]

      See identical proteins and their annotated locations for NP_414970.1

      Status: PROVISIONAL

      UniProtKB/TrEMBL
      A0A5B9APG2
      Conserved Domains (1) summary
      PRK01490
      Location:1 → 429
      tig; trigger factor; Provisional
    Nucleotide Protein
    Heading Accession and Version

    Gene LinkOut

    The following LinkOut resources are supplied by external providers. These providers are responsible for maintaining the links.