Difference between revisions of "Spx"
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| ===Phenotypes of a mutant === | ===Phenotypes of a mutant === | ||
| − | + | * Loss of up-regulation of the methionine sulfoxide reductase (''[[msrA]]-[[msrB]]'') operon in response to thiol specific oxidative stress, also loss of ''[[trxA]]'' and ''[[trxB]]'' upregulation in response to thiol specific oxidative stress. | |
| − | Loss of up-regulation of the methionine sulfoxide reductase (''[[msrA]]-[[msrB]]'') operon in response to thiol specific oxidative stress, also loss of ''[[trxA]]'' and ''[[trxB]]'' upregulation in response to thiol specific oxidative stress. | ||
| === Database entries === | === Database entries === | ||
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| '''Additional reviews:''' {{PubMed|20626317}} | '''Additional reviews:''' {{PubMed|20626317}} | ||
| ==The [[Spx regulon]]== | ==The [[Spx regulon]]== | ||
| − | <pubmed> 15937167, 14597697, 15028674, </pubmed> | + | <pubmed> 15937167, 14597697, 15028674, 22904090 </pubmed> | 
| ==Structural analysis of Spx== | ==Structural analysis of Spx== | ||
| <pubmed> 19580872, 16249335, </pubmed> | <pubmed> 19580872, 16249335, </pubmed> | ||
Revision as of 15:56, 22 August 2012
-  Description: transcriptional regulator Spx, involved in regulation of many genes. 
| Gene name | spx | 
| Synonyms | yjbD | 
| Essential | no | 
| Product | transcriptional regulator Spx | 
| Function | negative and positive regulator of many genes | 
| Gene expression levels in SubtiExpress: spx | |
| Interactions involving this protein in SubtInteract: Spx | |
| Metabolic function and regulation of this protein in SubtiPathways: Riboflavin / FAD | |
| MW, pI | 15,5 kDa, 7.80 | 
| Gene length, protein length | 393 bp, 131 amino acids | 
| Immediate neighbours | yjbC, yjbE | 
| Get the DNA and protein sequences (Barbe et al., 2009) | |
| Genetic context    This image was kindly provided by SubtiList | |
| Expression at a glance   PubMed   | |
Contents
Categories containing this gene/protein
transcription factors and their control, general stress proteins (controlled by SigB), cell envelope stress proteins (controlled by SigM, V, W, X, Y)
This gene is a member of the following regulons
PerR regulon, SigB regulon, SigM regulon, SigW regulon, SigX regulon
The Spx regulon
The gene
Basic information
- Locus tag: BSU11500
Phenotypes of a mutant
- Loss of up-regulation of the methionine sulfoxide reductase (msrA-msrB) operon in response to thiol specific oxidative stress, also loss of trxA and trxB upregulation in response to thiol specific oxidative stress.
Database entries
- DBTBS entry: [1]
- SubtiList entry: link
Additional information
The protein
Basic information/ Evolution
-  Catalyzed reaction/ biological activity: 
- transcriptional regulator of many genes in response to thiol specific oxidative stress (transcription activator of trxA and trxB)
- in addition, Spx inhibits transcription by binding to the C-terminal domain of the alpha subunit of RNAP (RpoA), disrupting complex formation between RNAP and certain transcriptional activator proteins like ResD and ComA
- in response to thiol specific oxidative stress, Spx can also activate transcription, making it a general regulator that exerts both positive and negative control over transcription initiation
- involved in competence regulation PubMed
 
- Protein family: Spx subfamily (according to Swiss-Prot) Arsenate Reductase (ArsC) family, Spx subfamily
- Paralogous protein(s): MgsR
Extended information on the protein
- Kinetic information:
- Domains: CXXC (10-13): Acts as a disulfide switch for the redox-sensitive transcriptional regulation of genes that function in thiol homeostasis.
- Modification: Cysteine oxidation of the CXXC motif
- Cofactor(s):
- Effectors of protein activity:
- Localization: cytoplasm (according to Swiss-Prot)
Database entries
- UniProt: O31602
- KEGG entry: [2]
- E.C. number:
Additional information
Expression and regulation
- Sigma factor:
- Regulation:
-  Additional information:
- post-translational control by ClpX-ClpP: Spx naturally contains a C-terminal sequence that resembles the SsrA tag and targets the protein for degradation. PubMed
- proteolysis is enhanced by YjbH PubMed and counter-acted by YirB PubMed
- the mRNA is substantially stabilized upon depletion of RNase Y (the half-life of the monocistronic spx mRNA increases from 1 to 6 min) PubMed
 
Biological materials
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody:
Labs working on this gene/protein
Peter Zuber, Oregon Health and Science University, USA Homepage
Richard Brennan, Houston, Texas, USA Homepage
Your additional remarks
References
Reviews
Additional reviews: PubMed
The Spx regulon
Tatiana Rochat, Pierre Nicolas, Olivier Delumeau, Alžbeta Rabatinová, Jana Korelusová, Aurélie Leduc, Philippe Bessières, Etienne Dervyn, Libor Krásny, Philippe Noirot  
Genome-wide identification of genes directly regulated by the pleiotropic transcription factor Spx in Bacillus subtilis. 
Nucleic Acids Res: 2012, 40(19);9571-83 
[PubMed:22904090]
  [WorldCat.org]
 [DOI]
 (I p)
Kyle N Erwin, Shunji Nakano, Peter Zuber  
Sulfate-dependent repression of genes that function in organosulfur metabolism in Bacillus subtilis requires Spx. 
J Bacteriol: 2005, 187(12);4042-9 
[PubMed:15937167]
  [WorldCat.org]
 [DOI]
 (P p)
Peter Zuber  
Spx-RNA polymerase interaction and global transcriptional control during oxidative stress. 
J Bacteriol: 2004, 186(7);1911-8 
[PubMed:15028674]
  [WorldCat.org]
 [DOI]
 (P p)
Shunji Nakano, Elke Küster-Schöck, Alan D Grossman, Peter Zuber  
Spx-dependent global transcriptional control is induced by thiol-specific oxidative stress in Bacillus subtilis. 
Proc Natl Acad Sci U S A: 2003, 100(23);13603-8 
[PubMed:14597697]
  [WorldCat.org]
 [DOI]
 (P p)
Structural analysis of Spx
Original Publications
Additional publications: PubMed
Lehnik-Habrink M, Schaffer M, Mäder U, Diethmaier C, Herzberg C, Stülke J RNA processing in Bacillus subtilis: identification of targets of the essential RNase Y. Mol Microbiol. 2011 81(6): 1459-1473. PubMed:21815947

