TrxA

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  • Description: thioredoxin, antioxidative action by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange, important for the prevention of protein aggregation during severe heat stress

Gene name trxA
Synonyms trx
Essential yes PubMed
Product thioredoxin
Function protection of proteins against oxidative damage
Gene expression levels in SubtiExpress: trxA
Interactions involving this protein in SubtInteract: TrxA
MW, pI 11 kDa, 4.308
Gene length, protein length 312 bp, 104 aa
Immediate neighbours uvrC, abf2
Sequences Protein DNA DNA_with_flanks
Genetic context
TrxA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
TrxA expression.png















Categories containing this gene/protein

electron transport/ other, general stress proteins (controlled by SigB), resistance against oxidative and electrophile stress, essential genes

This gene is a member of the following regulons

CtsR regulon, SigB regulon, Spx regulon

The gene

Basic information

  • Locus tag: BSU28500

Phenotypes of a mutant

essential PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

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

Extended information on the protein

  • Kinetic information:
  • Modification:
  • Effectors of protein activity:

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
    • induced by stress (SigB) PubMed
    • regulation by Spx in response to diamide stress
    • induced by heat stress (CtsR) PubMed
  • Regulatory mechanism:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Jun Lu, Arne Holmgren
The thioredoxin antioxidant system.
Free Radic Biol Med: 2014, 66;75-87
[PubMed:23899494] [WorldCat.org] [DOI] (I p)

Original publications

Stephanie Runde, Noël Molière, Anja Heinz, Etienne Maisonneuve, Armgard Janczikowski, Alexander K W Elsholz, Ulf Gerth, Michael Hecker, Kürşad Turgay
The role of thiol oxidative stress response in heat-induced protein aggregate formation during thermotolerance in Bacillus subtilis.
Mol Microbiol: 2014, 91(5);1036-52
[PubMed:24417481] [WorldCat.org] [DOI] (I p)

Mackenzie J Parker, Xuling Zhu, JoAnne Stubbe
Bacillus subtilis class Ib ribonucleotide reductase: high activity and dynamic subunit interactions.
Biochemistry: 2014, 53(4);766-76
[PubMed:24401092] [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)

Michiko M Nakano, Ann Lin, Cole S Zuber, Kate J Newberry, Richard G Brennan, Peter Zuber
Promoter recognition by a complex of Spx and the C-terminal domain of the RNA polymerase alpha subunit.
PLoS One: 2010, 5(1);e8664
[PubMed:20084284] [WorldCat.org] [DOI] (I e)

Dindo Y Reyes, Peter Zuber
Activation of transcription initiation by Spx: formation of transcription complex and identification of a Cis-acting element required for transcriptional activation.
Mol Microbiol: 2008, 69(3);765-79
[PubMed:18687074] [WorldCat.org] [DOI] (I p)

Jörg Mostertz, Falko Hochgräfe, Britta Jürgen, Thomas Schweder, Michael Hecker
The role of thioredoxin TrxA in Bacillus subtilis: a proteomics and transcriptomics approach.
Proteomics: 2008, 8(13);2676-90
[PubMed:18601268] [WorldCat.org] [DOI] (I p)

Mirja Carlsson Möller, Lars Hederstedt
Extracytoplasmic processes impaired by inactivation of trxA (thioredoxin gene) in Bacillus subtilis.
J Bacteriol: 2008, 190(13);4660-5
[PubMed:18456801] [WorldCat.org] [DOI] (I p)

Thijs R H M Kouwen, Annemieke van der Goot, Ronald Dorenbos, Theresa Winter, Haike Antelmann, Marie-Claire Plaisier, Wim J Quax, January Maarten van Dijl, Jean-Yves F Dubois
Thiol-disulphide oxidoreductase modules in the low-GC Gram-positive bacteria.
Mol Microbiol: 2007, 64(4);984-99
[PubMed:17501922] [WorldCat.org] [DOI] (P p)

You Li, Yunfei Hu, Xinxin Zhang, Huimin Xu, Ewen Lescop, Bin Xia, Changwen Jin
Conformational fluctuations coupled to the thiol-disulfide transfer between thioredoxin and arsenate reductase in Bacillus subtilis.
J Biol Chem: 2007, 282(15);11078-83
[PubMed:17303556] [WorldCat.org] [DOI] (P p)

Wiep Klaas Smits, Jean-Yves F Dubois, Sierd Bron, Jan Maarten van Dijl, Oscar P Kuipers
Tricksy business: transcriptome analysis reveals the involvement of thioredoxin A in redox homeostasis, oxidative stress, sulfur metabolism, and cellular differentiation in Bacillus subtilis.
J Bacteriol: 2005, 187(12);3921-30
[PubMed:15937154] [WorldCat.org] [DOI] (P p)

Shunji Nakano, Michiko M Nakano, Ying Zhang, Montira Leelakriangsak, Peter Zuber
A regulatory protein that interferes with activator-stimulated transcription in bacteria.
Proc Natl Acad Sci U S A: 2003, 100(7);4233-8
[PubMed:12642660] [WorldCat.org] [DOI] (P p)

A Petersohn, M Brigulla, S Haas, J D Hoheisel, U Völker, M Hecker
Global analysis of the general stress response of Bacillus subtilis.
J Bacteriol: 2001, 183(19);5617-31
[PubMed:11544224] [WorldCat.org] [DOI] (P p)

E Krüger, M Hecker
The first gene of the Bacillus subtilis clpC operon, ctsR, encodes a negative regulator of its own operon and other class III heat shock genes.
J Bacteriol: 1998, 180(24);6681-8
[PubMed:9852015] [WorldCat.org] [DOI] (P p)

C Scharf, S Riethdorf, H Ernst, S Engelmann, U Völker, M Hecker
Thioredoxin is an essential protein induced by multiple stresses in Bacillus subtilis.
J Bacteriol: 1998, 180(7);1869-77
[PubMed:9537387] [WorldCat.org] [DOI] (P p)

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