Difference between revisions of "SigB"
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=== Additional information=== | === Additional information=== | ||
− | + | * mutations in ''[[mtrB]]'', ''[[sigB]]'', ''[[rpoB]]'', and ''[[rpoC]]'' allow ''B. subtilis'' to grow with 4-fluorotryptophan rather than with tryptophan as a canonical amino acid of the genetic code {{PubMed|24572018}} | |
− | |||
− | |||
=The protein= | =The protein= | ||
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* '''Kinetic information:''' | * '''Kinetic information:''' | ||
− | * '''Domains:''' | + | * '''[[Domains]]:''' |
* '''Modification:''' | * '''Modification:''' | ||
− | * ''' | + | * '''[[Cofactors]]:''' |
* '''Effectors of protein activity:''' | * '''Effectors of protein activity:''' | ||
Line 162: | Line 160: | ||
<pubmed> 11544224, 11532142, 11717291, 10482513, 10220166,22174379 </pubmed> | <pubmed> 11544224, 11532142, 11717291, 10482513, 10220166,22174379 </pubmed> | ||
==Other publications== | ==Other publications== | ||
− | <pubmed>23407164,22511268,22210769 23524614 21979936 8655572,, 3123466, 10369900,3112122, 8468294,8458834, 13129942, 6784117, 12867438, 3100810, 8253681, 12486038, 8764398,3027048, 15342585,17575448, 17586624,23934352, 3016731,11902719,14651641,10503549,15205443,6405278, 10383961, 15805528 6790515 116131, 39767581 19948797 22582280</pubmed> | + | <pubmed>23407164,22511268,22210769 23524614 21979936 8655572,, 3123466, 10369900,3112122, 8468294,8458834, 13129942, 6784117, 12867438, 3100810, 8253681, 12486038, 8764398,3027048, 15342585,17575448, 17586624,23934352, 3016731,11902719,14651641,10503549,15205443,6405278, 10383961, 15805528 6790515 116131, 39767581 19948797 22582280 24572018</pubmed> |
[[Category:Protein-coding genes]] | [[Category:Protein-coding genes]] |
Revision as of 16:22, 28 February 2014
- Description: RNA polymerase sigma factor SigB
Gene name | sigB |
Synonyms | rpoF |
Essential | no |
Product | RNA polymerase sigma factor SigB |
Function | general stress response |
Gene expression levels in SubtiExpress: sigB | |
Interactions involving this protein in SubtInteract: SigB | |
Metabolic function and regulation of this protein in SubtiPathways: sigB | |
MW, pI | 29 kDa, 5.418 |
Gene length, protein length | 792 bp, 264 aa |
Immediate neighbours | rsbW, rsbX |
Sequences | Protein DNA DNA_with_flanks |
Genetic context This image was kindly provided by SubtiList
| |
Expression at a glance PubMed |
Contents
Categories containing this gene/protein
transcription, sigma factors and their control, general stress proteins (controlled by SigB)
This gene is a member of the following regulons
The SigB regulon
The gene
Basic information
- Locus tag: BSU04730
Phenotypes of a mutant
Database entries
- DBTBS entry: [1]
- SubtiList entry: [2]
Additional information
- mutations in mtrB, sigB, rpoB, and rpoC allow B. subtilis to grow with 4-fluorotryptophan rather than with tryptophan as a canonical amino acid of the genetic code PubMed
The protein
Basic information/ Evolution
- Catalyzed reaction/ biological activity:
- Protein family: SigB subfamily (according to Swiss-Prot)
- Paralogous protein(s):
Extended information on the protein
- Kinetic information:
- Modification:
- Effectors of protein activity:
Database entries
- Structure:
- UniProt: P06574
- KEGG entry: [3]
- E.C. number:
Additional information
Expression and regulation
- Additional information:
Biological materials
- Mutant: QB5344 (cat), available in the Stülke lab
- Expression vector:
- lacZ fusion:
- GFP fusion:
- two-hybrid system:
- Antibody:
Labs working on this gene/protein
- Bill Haldenwang, San Antonio, USA
- Chet Price, Davis, USA homepage
Your additional remarks
References
Reviews
Jon Marles-Wright, Richard J Lewis
The stressosome: molecular architecture of a signalling hub.
Biochem Soc Trans: 2010, 38(4);928-33
[PubMed:20658979]
[WorldCat.org]
[DOI]
(I p)
Peter Zuber
Management of oxidative stress in Bacillus.
Annu Rev Microbiol: 2009, 63;575-97
[PubMed:19575568]
[WorldCat.org]
[DOI]
(I p)
Michael Hecker, Jan Pané-Farré, Uwe Völker
SigB-dependent general stress response in Bacillus subtilis and related gram-positive bacteria.
Annu Rev Microbiol: 2007, 61;215-36
[PubMed:18035607]
[WorldCat.org]
[DOI]
(P p)
M Hecker, U Völker
General stress response of Bacillus subtilis and other bacteria.
Adv Microb Physiol: 2001, 44;35-91
[PubMed:11407115]
[WorldCat.org]
[DOI]
(P p)
M Hecker, U Völker
Non-specific, general and multiple stress resistance of growth-restricted Bacillus subtilis cells by the expression of the sigmaB regulon.
Mol Microbiol: 1998, 29(5);1129-36
[PubMed:9767581]
[WorldCat.org]
[DOI]
(P p)
Control of SigB activity by protein-protein interactions
Oleg A Igoshin, Margaret S Brody, Chester W Price, Michael A Savageau
Distinctive topologies of partner-switching signaling networks correlate with their physiological roles.
J Mol Biol: 2007, 369(5);1333-52
[PubMed:17498739]
[WorldCat.org]
[DOI]
(P p)
Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
In vivo phosphorylation of partner switching regulators correlates with stress transmission in the environmental signaling pathway of Bacillus subtilis.
J Bacteriol: 2004, 186(18);6124-32
[PubMed:15342582]
[WorldCat.org]
[DOI]
(P p)
Tae-Jong Kim, Tatiana A Gaidenko, Chester W Price
A multicomponent protein complex mediates environmental stress signaling in Bacillus subtilis.
J Mol Biol: 2004, 341(1);135-50
[PubMed:15312768]
[WorldCat.org]
[DOI]
(P p)
Olivier Delumeau, Richard J Lewis, Michael D Yudkin
Protein-protein interactions that regulate the energy stress activation of sigma(B) in Bacillus subtilis.
J Bacteriol: 2002, 184(20);5583-9
[PubMed:12270815]
[WorldCat.org]
[DOI]
(P p)
M S Brody, K Vijay, C W Price
Catalytic function of an alpha/beta hydrolase is required for energy stress activation of the sigma(B) transcription factor in Bacillus subtilis.
J Bacteriol: 2001, 183(21);6422-8
[PubMed:11591687]
[WorldCat.org]
[DOI]
(P p)
C Eymann, M Hecker
Induction of sigma(B)-dependent general stress genes by amino acid starvation in a spo0H mutant of Bacillus subtilis.
FEMS Microbiol Lett: 2001, 199(2);221-7
[PubMed:11377871]
[WorldCat.org]
[DOI]
(P p)
A Dufour, U Voelker, A Voelker, W G Haldenwang
Relative levels and fractionation properties of Bacillus subtilis σ(B) and its regulators during balanced growth and stress.
J Bacteriol: 1996, 178(13);3701-9 sigma
[PubMed:8682769]
[WorldCat.org]
[DOI]
(P p)
U Voelker, A Voelker, B Maul, M Hecker, A Dufour, W G Haldenwang
Separate mechanisms activate sigma B of Bacillus subtilis in response to environmental and metabolic stresses.
J Bacteriol: 1995, 177(13);3771-80
[PubMed:7601843]
[WorldCat.org]
[DOI]
(P p)
A A Wise, C W Price
Four additional genes in the sigB operon of Bacillus subtilis that control activity of the general stress factor sigma B in response to environmental signals.
J Bacteriol: 1995, 177(1);123-33
[PubMed:8002610]
[WorldCat.org]
[DOI]
(P p)
A K Benson, W G Haldenwang
Bacillus subtilis sigma B is regulated by a binding protein (RsbW) that blocks its association with core RNA polymerase.
Proc Natl Acad Sci U S A: 1993, 90(6);2330-4
[PubMed:8460143]
[WorldCat.org]
[DOI]
(P p)
Identification of the SigB regulon
Other publications