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

Original publications

Irnov Irnov, Cynthia M Sharma, Jörg Vogel, Wade C Winkler
Identification of regulatory RNAs in Bacillus subtilis.
Nucleic Acids Res: 2010, 38(19);6637-51
[PubMed:20525796] [WorldCat.org] [DOI] (I p)

Frieder Merz, Daniel Boehringer, Christiane Schaffitzel, Steffen Preissler, Anja Hoffmann, Timm Maier, Anna Rutkowska, Jasmin Lozza, Nenad Ban, Bernd Bukau, Elke Deuerling
Molecular mechanism and structure of Trigger Factor bound to the translating ribosome.
EMBO J: 2008, 27(11);1622-32
[PubMed:18497744] [WorldCat.org] [DOI] (I p)

Alain Lévine, Françoise Vannier, Cédric Absalon, Lauriane Kuhn, Peter Jackson, Elaine Scrivener, Valérie Labas, Joëlle Vinh, Patrick Courtney, Jérôme Garin, Simone J Séror
Analysis of the dynamic Bacillus subtilis Ser/Thr/Tyr phosphoproteome implicated in a wide variety of cellular processes.
Proteomics: 2006, 6(7);2157-73
[PubMed:16493705] [WorldCat.org] [DOI] (P p)

Dindo Y Reyes, Hirofumi Yoshikawa
DnaK chaperone machine and trigger factor are only partially required for normal growth of Bacillus subtilis.
Biosci Biotechnol Biochem: 2002, 66(7);1583-6
[PubMed:12224648] [WorldCat.org] [DOI] (P p)

S F Göthel, C Scholz, F X Schmid, M A Marahiel
Cyclophilin and trigger factor from Bacillus subtilis catalyze in vitro protein folding and are necessary for viability under starvation conditions.
Biochemistry: 1998, 37(38);13392-9
[PubMed:9748346] [WorldCat.org] [DOI] (P p)

S F Göthel, R Schmid, A Wipat, N M Carter, P T Emmerson, C R Harwood, M A Marahiel
An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor.
Eur J Biochem: 1997, 244(1);59-65
[PubMed:9063446] [WorldCat.org] [DOI] (P p)

A Wipat, N Carter, S C Brignell, B J Guy, K Piper, J Sanders, P T Emmerson, C R Harwood
The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism.
Microbiology (Reading): 1996, 142 ( Pt 11);3067-78
[PubMed:8969504] [WorldCat.org] [DOI] (P p)