Difference between revisions of "Tig"

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= Categories containing this gene/protein =
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{{SubtiWiki category|[[chaperones/ protein folding]]}},
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{{SubtiWiki category|[[phosphoproteins]]}}
 
=The protein=
 
=The protein=
  

Revision as of 20:34, 30 November 2010

  • Description: trigger factor (prolyl isomerase)

Gene name tig
Synonyms yzzH
Essential no
Product trigger factor (prolyl isomerase)
Function protein folding
MW, pI 47 kDa, 4.224
Gene length, protein length 1272 bp, 424 aa
Immediate neighbours clpX, ysoA
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Tig context.gif
This image was kindly provided by SubtiList



The gene

Basic information

  • Locus tag: BSU28230

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

Categories containing this gene/protein

chaperones/ protein folding, phosphoproteins

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity:
  • Protein family: Tig subfamily (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification: phosphorylated on ser/ thr/ tyr PubMed
  • Cofactor(s):
  • Effectors of protein activity:
  • Interactions:
  • Localization:

Database entries

  • Structure: 2VRH (the E. coli trigger factor) PubMed
  • KEGG entry: [3]
  • E.C. number:

Additional information

  • subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

  • Regulation:
    • RelA dependent downregulation (Class I) during stringent response PubMed
  • Regulatory mechanism:
  • Additional information:
    • subject to Clp-dependent proteolysis upon glucose starvation PubMed
    • The mRNA has a long 5' leader region. This may indicate RNA-based regulation PubMed

Biological materials

  • Mutant:
  • Expression vector:
  • lacZ fusion:
  • GFP fusion:
  • two-hybrid system:
  • Antibody:

Labs working on this gene/protein

Your additional remarks

References

Reviews

Carmela Giglione, Sonia Fieulaine, Thierry Meinnel
Cotranslational processing mechanisms: towards a dynamic 3D model.
Trends Biochem Sci: 2009, 34(8);417-26
[PubMed:19647435] [WorldCat.org] [DOI] (I p)

R D Wegrzyn, E Deuerling
Molecular guardians for newborn proteins: ribosome-associated chaperones and their role in protein folding.
Cell Mol Life Sci: 2005, 62(23);2727-38
[PubMed:16231086] [WorldCat.org] [DOI] (P p)

Timm Maier, Lars Ferbitz, Elke Deuerling, Nenad Ban
A cradle for new proteins: trigger factor at the ribosome.
Curr Opin Struct Biol: 2005, 15(2);204-12
[PubMed:15837180] [WorldCat.org] [DOI] (P p)

Elke Deuerling, Bernd Bukau
Chaperone-assisted folding of newly synthesized proteins in the cytosol.
Crit Rev Biochem Mol Biol: 2004, 39(5-6);261-77
[PubMed:15763705] [WorldCat.org] [DOI] (P p)

Original publications