Difference between revisions of "CitB"
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* '''Expression vector:''' | * '''Expression vector:''' | ||
− | * '''lacZ fusion:''' | + | * '''lacZ fusion:''' pGP700 (in [[pAC5]]), available in [[Stülke]] lab |
* '''GFP fusion:''' | * '''GFP fusion:''' |
Revision as of 18:16, 29 October 2009
- Description: trigger enzyme: aconitase and RNA binding protein
Gene name | citB |
Synonyms | |
Essential | no |
Product | trigger enzyme: aconitate hydratase (aconitase) |
Function | TCA cycle |
Metabolic function and regulation of this protein in SubtiPathways: Central C-metabolism | |
MW, pI | 99 kDa, 4.903 |
Gene length, protein length | 2727 bp, 909 aa |
Immediate neighbours | sspO, yneN |
Get the DNA and protein sequences (Barbe et al., 2009) | |
Genetic context This image was kindly provided by SubtiList
|
Contents
The gene
Basic information
- Locus tag: BSU18000
Phenotypes of a mutant
glutamate auxotrophy and a defect in sporulation PubMed
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity: Citrate = isocitrate (according to Swiss-Prot)
- Binding to iron responsive elements (IRE RNA) in the absence of the FeS cluster PubMed
- Protein family:
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Domains:
- Modification:
- Cofactor(s): FeS cluster
- Effectors of protein activity:
- Interactions:
- Localization:
Database entries
- Structure: 1L5J (E. coli)
- UniProt: P09339
- KEGG entry: [3]
- E.C. number: 4.2.1.3
Additional information
B. subtilis aconitase is both an enzyme and an RNA binding protein PubMed
Expression and regulation
- Regulation:
- repressed during growth in the presence of branched chain amino acids (CodY) PubMed
- repressed in the presence of glucose and glutamate (CcpC) PubMed
- expressed upon transition into the stationary phase (AbrB) PubMed
- repressed by glucose (3.7-fold) (CcpA) PubMed
- repression by glucose + arginine (CcpC) PubMed
- less expressed under conditions of extreme iron limitation (FsrA) PubMed
- Regulatory mechanism:
- Additional information:
Biological materials
- Mutant: GP683 (erm), available in Stülke lab
- Expression vector:
- GFP fusion:
- two-hybrid system: B. pertussis adenylate cyclase-based bacterial two hybrid system (BACTH), available in Stülke lab
- Antibody: available in Linc Sonenshein lab
Labs working on this gene/protein
Linc Sonenshein, Tufts University, Boston, MA, USA Homepage
Jörg Stülke, University of Göttingen, Germany Homepage
Your additional remarks
References
Ahmed Gaballa, Haike Antelmann, Claudio Aguilar, Sukhjit K Khakh, Kyung-Bok Song, Gregory T Smaldone, John D Helmann
The Bacillus subtilis iron-sparing response is mediated by a Fur-regulated small RNA and three small, basic proteins.
Proc Natl Acad Sci U S A: 2008, 105(33);11927-32
[PubMed:18697947]
[WorldCat.org]
[DOI]
(I p)
Alisa W Serio, Kieran B Pechter, Abraham L Sonenshein
Bacillus subtilis aconitase is required for efficient late-sporulation gene expression.
J Bacteriol: 2006, 188(17);6396-405
[PubMed:16923907]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Irene Reif, Fabian M Commichau, Christian Detsch, Ingrid Wacker, Holger Ludwig, Jörg Stülke
Regulation of citB expression in Bacillus subtilis: integration of multiple metabolic signals in the citrate pool and by the general nitrogen regulatory system.
Arch Microbiol: 2006, 185(2);136-46
[PubMed:16395550]
[WorldCat.org]
[DOI]
(P p)
Hans-Matti Blencke, Georg Homuth, Holger Ludwig, Ulrike Mäder, Michael Hecker, Jörg Stülke
Transcriptional profiling of gene expression in response to glucose in Bacillus subtilis: regulation of the central metabolic pathways.
Metab Eng: 2003, 5(2);133-49
[PubMed:12850135]
[WorldCat.org]
[DOI]
(P p)
Hyun-Jin Kim, Sam-In Kim, Manoja Ratnayake-Lecamwasam, Kiyoshi Tachikawa, Abraham L Sonenshein, Mark Strauch
Complex regulation of the Bacillus subtilis aconitase gene.
J Bacteriol: 2003, 185(5);1672-80
[PubMed:12591885]
[WorldCat.org]
[DOI]
(P p)
C Jourlin-Castelli, N Mani, M M Nakano, A L Sonenshein
CcpC, a novel regulator of the LysR family required for glucose repression of the citB gene in Bacillus subtilis.
J Mol Biol: 2000, 295(4);865-78
[PubMed:10656796]
[WorldCat.org]
[DOI]
(P p)
C Alén, A L Sonenshein
Bacillus subtilis aconitase is an RNA-binding protein.
Proc Natl Acad Sci U S A: 1999, 96(18);10412-7
[PubMed:10468622]
[WorldCat.org]
[DOI]
(P p)
M M Nakano, P Zuber, A L Sonenshein
Anaerobic regulation of Bacillus subtilis Krebs cycle genes.
J Bacteriol: 1998, 180(13);3304-11
[PubMed:9642180]
[WorldCat.org]
[DOI]
(P p)
J E Craig, M J Ford, D C Blaydon, A L Sonenshein
A null mutation in the Bacillus subtilis aconitase gene causes a block in Spo0A-phosphate-dependent gene expression.
J Bacteriol: 1997, 179(23);7351-9
[PubMed:9393699]
[WorldCat.org]
[DOI]
(P p)
A Fouet, S F Jin, G Raffel, A L Sonenshein
Multiple regulatory sites in the Bacillus subtilis citB promoter region.
J Bacteriol: 1990, 172(9);5408-15
[PubMed:2118511]
[WorldCat.org]
[DOI]
(P p)
A Fouet, A L Sonenshein
A target for carbon source-dependent negative regulation of the citB promoter of Bacillus subtilis.
J Bacteriol: 1990, 172(2);835-44
[PubMed:2105305]
[WorldCat.org]
[DOI]
(P p)
M S Rosenkrantz, D W Dingman, A L Sonenshein
Bacillus subtilis citB gene is regulated synergistically by glucose and glutamine.
J Bacteriol: 1985, 164(1);155-64
[PubMed:2413006]
[WorldCat.org]
[DOI]
(P p)
S H Fisher, B Magasanik
2-Ketoglutarate and the regulation of aconitase and histidase formation in Bacillus subtilis.
J Bacteriol: 1984, 158(1);379-82
[PubMed:6143742]
[WorldCat.org]
[DOI]
(P p)