Difference between revisions of "Tig"

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|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28230 tig]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU28230 tig]
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|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Tig Tig]
 
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|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 47 kDa, 4.224   
 
|style="background:#ABCDEF;" align="center"| '''MW, pI''' || 47 kDa, 4.224   
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* '''[[SubtInteract|Interactions]]:'''
 
* '''[[SubtInteract|Interactions]]:'''
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** [[Tig]]-[[RplW]] {{PubMed|16271892,16091460}}
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** [[Tig]]-[[RpmC]] {{PubMed|16271892,16091460}}
  
 
* '''[[Localization]]:'''
 
* '''[[Localization]]:'''
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<pubmed>16231086 15763705 15837180 19647435 </pubmed>
 
<pubmed>16231086 15763705 15837180 19647435 </pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>12224648,9748346,9063446,18497744 ,16493705, 8969504 20525796 22517742</pubmed>
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<pubmed>12224648,9748346,9063446,18497744 ,16493705, 8969504 20525796 22517742 16271892,16091460</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 12:10, 20 August 2013

  • Description: trigger factor (prolyl isomerase)

Gene name tig
Synonyms yzzH
Essential no
Product trigger factor (prolyl isomerase)
Function protein folding
Gene expression levels in SubtiExpress: tig
Interactions involving this protein in SubtInteract: Tig
MW, pI 47 kDa, 4.224
Gene length, protein length 1272 bp, 424 aa
Immediate neighbours clpX, ysoA
Sequences Protein DNA DNA_with_flanks
Genetic context
Tig context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Tig expression.png















Categories containing this gene/protein

chaperones/ protein folding, phosphoproteins

This gene is a member of the following regulons

stringent response

The gene

Basic information

  • Locus tag: BSU28230

Phenotypes of a mutant

Database entries

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

Additional information

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 Arg-90 PubMed
    • phosphorylated on ser/ thr/ tyr PubMed
  • Cofactor(s):
  • Effectors of protein activity:

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

  • Sigma factor:
  • 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