Tig

• 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 This image was kindly provided by SubtiList
Expression at a glance   PubMed

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

Database entries

• DBTBS entry: [1]

• SubtiList entry: [2]

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:

• Interactions:
  • Tig-RplW PubMed
  • Tig-RpmC PubMed

• Localization:

Database entries

• Structure: 2VRH (the E. coli trigger factor) PubMed

• UniProt: P80698

• KEGG entry: [3]

• E.C. number:

Additional information

• subject to Clp-dependent proteolysis upon glucose starvation PubMed

Expression and regulation

• Operon: tig PubMed

• Expression browser: tig PubMed

• 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:

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

Alexander K W Elsholz, Kürsad Turgay, Stephan Michalik, Bernd Hessling, Katrin Gronau, Dan Oertel, Ulrike Mäder, Jörg Bernhardt, Dörte Becher, Michael Hecker, Ulf Gerth
Global impact of protein arginine phosphorylation on the physiology of Bacillus subtilis.
Proc Natl Acad Sci U S A: 2012, 109(19);7451-6
[PubMed:22517742] [WorldCat.org] [DOI] (I p)

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)

Frank Schlünzen, Daniel N Wilson, Pingsheng Tian, Jörg M Harms, Stuart J McInnes, Harly A S Hansen, Renate Albrecht, Jörg Buerger, Sigurd M Wilbanks, Paola Fucini
The binding mode of the trigger factor on the ribosome: implications for protein folding and SRP interaction.
Structure: 2005, 13(11);1685-94
[PubMed:16271892] [WorldCat.org] [DOI] (P p)

David Baram, Erez Pyetan, Assa Sittner, Tamar Auerbach-Nevo, Anat Bashan, Ada Yonath
Structure of trigger factor binding domain in biologically homologous complex with eubacterial ribosome reveals its chaperone action.
Proc Natl Acad Sci U S A: 2005, 102(34);12017-22
[PubMed:16091460] [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)