Difference between revisions of "TrxA"

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(References)
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* '''Effectors of protein activity:'''
 
* '''Effectors of protein activity:'''
  
* '''Interactions:''' [[TrxA]]-[[ArsC]]
+
* '''Interactions:''' [[ArsC]]-[[TrxA]] {{PubMed|17303556}}
  
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
 
* '''Localization:''' cytoplasm (according to Swiss-Prot)
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=== Database entries ===
 
=== Database entries ===
  
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2GZZ 2GZZ] (oxidized form),  [http://www.rcsb.org/pdb/explore.do?structureId=2GZY 2GZY] (reduced form),  [http://www.rcsb.org/pdb/explore.do?structureId=2IPA 2IPA] (TrxA-ArsC-complex)
+
* '''Structure:''' [http://www.rcsb.org/pdb/explore.do?structureId=2GZZ 2GZZ] (oxidized form),  [http://www.rcsb.org/pdb/explore.do?structureId=2GZY 2GZY] (reduced form),  [http://www.rcsb.org/pdb/explore.do?structureId=2IPA 2IPA] (TrxA-ArsC-complex) {{PubMed|17303556}}
  
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P14949 P14949]
 
* '''UniProt:''' [http://www.uniprot.org/uniprot/P14949 P14949]
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=References=
 
=References=
  
<pubmed>9537387,15937154,18601268,18456801,9852015 ,11544224,18687074 20084284 </pubmed>
+
<pubmed>9537387,15937154,18601268,18456801,9852015 ,11544224,18687074 20084284 17303556</pubmed>
  
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 06:40, 24 February 2010

  • Description: antioxidative action by facilitating the reduction of other proteins by cysteine thiol-disulfide exchange

Gene name trxA
Synonyms trx
Essential yes PubMed
Product thioredoxin
Function protection of proteins against oxidative damage
MW, pI 11 kDa, 4.308
Gene length, protein length 312 bp, 104 aa
Immediate neighbours uvrC, abf2
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
TrxA context.gif
This image was kindly provided by SubtiList



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:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:
  • Localization: cytoplasm (according to Swiss-Prot)

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:
  • Additional information:

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

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)

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)

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)