Difference between revisions of "SigA"

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** [[BsrB]]-[[SigA]]-[[RNA polymerase]]
 
** [[BsrB]]-[[SigA]]-[[RNA polymerase]]
  
−
* '''[[Localization]]:''' cell membrane (according to Swiss-Prot)
+
* '''[[Localization]]:'''
 +
** cytoplasm {{PubMed|25313396}}
  
 
=== Database entries ===
 
=== Database entries ===

Revision as of 16:40, 27 October 2014

Gene name sigA
Synonyms rpoD, crsA
Essential yes PubMed
Product RNA polymerase major sigma factor SigA
Function transcription
Gene expression levels in SubtiExpress: sigA
Interactions involving this protein in SubtInteract: SigA
MW, pI 42 kDa, 4.634
Gene length, protein length 1113 bp, 371 aa
Immediate neighbours cccA, dnaG
Sequences Protein DNA DNA_with_flanks
Genetic context
SigA context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
SigA expression.png















Categories containing this gene/protein

transcription, sigma factors and their control, essential genes, membrane proteins

This gene is a member of the following regulons

SigD regulon, SigH regulon

The gene

Basic information

  • Locus tag: BSU25200

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: sigma-70 factor family (according to Swiss-Prot)
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
  • Effectors of protein activity:

Database entries

  • Structure:
  • KEGG entry: [3]
  • E.C. number:

Additional information

Expression and regulation

  • Regulation:
  • Regulatory mechanism:
  • Additional information:
    • An antisense RNA is predicted for sigA PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium): 802 PubMed
    • number of protein molecules per cell (complex medium with amino acids, without glucose): 1811 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, exponential phase): 1136 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, early stationary phase after glucose exhaustion): 2062 PubMed
    • number of protein molecules per cell (minimal medium with glucose and ammonium, late stationary phase after glucose exhaustion): 1407 PubMed

Biological materials

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

Labs working on this gene/protein

Your additional remarks

References

Reviews

Benedikt Steuten, Sabine Schneider, Rolf Wagner
6S RNA: recent answers--future questions.
Mol Microbiol: 2014, 91(4);641-8
[PubMed:24308327] [WorldCat.org] [DOI] (I p)

Lakshminarayan M Iyer, L Aravind
Insights from the architecture of the bacterial transcription apparatus.
J Struct Biol: 2012, 179(3);299-319
[PubMed:22210308] [WorldCat.org] [DOI] (I p)


Original publications

Yong Heon Lee, John D Helmann
Mutations in the primary sigma factor σA and termination factor rho that reduce susceptibility to cell wall antibiotics.
J Bacteriol: 2014, 196(21);3700-11
[PubMed:25112476] [WorldCat.org] [DOI] (I p)

Hsin-Yi Yeh, Hsiu-Ting Hsu, Tsung-Ching Chen, Kuei-Min Chung, Kung-Ming Liou, Ban-Yang Chang
The reduction in σ-promoter recognition flexibility as induced by core RNAP is required for σ to discern the optimal promoter spacing.
Biochem J: 2013, 455(2);185-93
[PubMed:23875654] [WorldCat.org] [DOI] (I p)

Benedikt M Beckmann, Philipp G Hoch, Manja Marz, Dagmar K Willkomm, Margarita Salas, Roland K Hartmann
A pRNA-induced structural rearrangement triggers 6S-1 RNA release from RNA polymerase in Bacillus subtilis.
EMBO J: 2012, 31(7);1727-38
[PubMed:22333917] [WorldCat.org] [DOI] (I p)

Hsin-Yi Yeh, Tsung-Ching Chen, Kung-Ming Liou, Hsiu-Ting Hsu, Kuei-Min Chung, Li-Ling Hsu, Ban-Yang Chang
The core-independent promoter-specific interaction of primary sigma factor.
Nucleic Acids Res: 2011, 39(3);913-25
[PubMed:20935043] [WorldCat.org] [DOI] (I p)

Shu Ishikawa, Taku Oshima, Ken Kurokawa, Yoko Kusuya, Naotake Ogasawara
RNA polymerase trafficking in Bacillus subtilis cells.
J Bacteriol: 2010, 192(21);5778-87
[PubMed:20817769] [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)

Elecia B Johnston, Peter J Lewis, Renate Griffith
The interaction of Bacillus subtilis sigmaA with RNA polymerase.
Protein Sci: 2009, 18(11);2287-97
[PubMed:19735077] [WorldCat.org] [DOI] (I p)

Xiao Yang, Seeseei Molimau, Geoff P Doherty, Elecia B Johnston, Jon Marles-Wright, Rosalba Rothnagel, Ben Hankamer, Richard J Lewis, Peter J Lewis
The structure of bacterial RNA polymerase in complex with the essential transcription elongation factor NusA.
EMBO Rep: 2009, 10(9);997-1002
[PubMed:19680289] [WorldCat.org] [DOI] (I p)

Steve D Seredick, George B Spiegelman
The Bacillus subtilis response regulator Spo0A stimulates sigmaA-dependent transcription prior to the major energetic barrier.
J Biol Chem: 2004, 279(17);17397-403
[PubMed:14976210] [WorldCat.org] [DOI] (P p)

Amrita Kumar, James A Brannigan, Charles P Moran
Alpha-helix E of Spo0A is required for sigmaA- but not for sigmaH-dependent promoter activation in Bacillus subtilis.
J Bacteriol: 2004, 186(4);1078-83
[PubMed:14762002] [WorldCat.org] [DOI] (P p)

Amrita Kumar, Cindy Buckner Starke, Mark DeZalia, Charles P Moran
Surfaces of Spo0A and RNA polymerase sigma factor A that interact at the spoIIG promoter in Bacillus subtilis.
J Bacteriol: 2004, 186(1);200-6
[PubMed:14679239] [WorldCat.org] [DOI] (P p)

Claudia Rollenhagen, Haike Antelmann, Janine Kirstein, Olivier Delumeau, Michael Hecker, Michael D Yudkin
Binding of sigma(A) and sigma(B) to core RNA polymerase after environmental stress in Bacillus subtilis.
J Bacteriol: 2003, 185(1);35-40
[PubMed:12486038] [WorldCat.org] [DOI] (P p)

Hanne Jarmer, Thomas S Larsen, Anders Krogh, Hans Henrik Saxild, Søren Brunak, Steen Knudsen
Sigma A recognition sites in the Bacillus subtilis genome.
Microbiology (Reading): 2001, 147(Pt 9);2417-2424
[PubMed:11535782] [WorldCat.org] [DOI] (P p)

J Qiu, J D Helmann
Adenines at -11, -9 and -8 play a key role in the binding of Bacillus subtilis Esigma(A) RNA polymerase to -10 region single-stranded DNA.
Nucleic Acids Res: 1999, 27(23);4541-6
[PubMed:10556308] [WorldCat.org] [DOI] (P p)

J Ju, T Mitchell, H Peters, W G Haldenwang
Sigma factor displacement from RNA polymerase during Bacillus subtilis sporulation.
J Bacteriol: 1999, 181(16);4969-77
[PubMed:10438769] [WorldCat.org] [DOI] (P p)

C M Buckner, G Schyns, C P Moran
A region in the Bacillus subtilis transcription factor Spo0A that is important for spoIIG promoter activation.
J Bacteriol: 1998, 180(14);3578-83
[PubMed:9658000] [WorldCat.org] [DOI] (P p)

G Schyns, C M Buckner, C P Moran
Activation of the Bacillus subtilis spoIIG promoter requires interaction of Spo0A and the sigma subunit of RNA polymerase.
J Bacteriol: 1997, 179(17);5605-8
[PubMed:9287022] [WorldCat.org] [DOI] (P p)

X Huang, F J Lopez de Saro, J D Helmann
sigma factor mutations affecting the sequence-selective interaction of RNA polymerase with -10 region single-stranded DNA.
Nucleic Acids Res: 1997, 25(13);2603-9
[PubMed:9185571] [WorldCat.org] [DOI] (P p)

K Fredrick, J D Helmann
RNA polymerase sigma factor determines start-site selection but is not required for upstream promoter element activation on heteroduplex (bubble) templates.
Proc Natl Acad Sci U S A: 1997, 94(10);4982-7
[PubMed:9144176] [WorldCat.org] [DOI] (P p)

J D Helmann
Compilation and analysis of Bacillus subtilis sigma A-dependent promoter sequences: evidence for extended contact between RNA polymerase and upstream promoter DNA.
Nucleic Acids Res: 1995, 23(13);2351-60
[PubMed:7630711] [WorldCat.org] [DOI] (P p)

Y L Juang, J D Helmann
Pathway of promoter melting by Bacillus subtilis RNA polymerase at a stable RNA promoter: effects of temperature, delta protein, and sigma factor mutations.
Biochemistry: 1995, 34(26);8465-73
[PubMed:7599136] [WorldCat.org] [DOI] (P p)

S E Aiyar, Y L Juang, J D Helmann, P L deHaseth
Mutations in sigma factor that affect the temperature dependence of transcription from a promoter, but not from a mismatch bubble in double-stranded DNA.
Biochemistry: 1994, 33(38);11501-6
[PubMed:7918363] [WorldCat.org] [DOI] (P p)

J C Rong, J D Helmann
Genetic and physiological studies of Bacillus subtilis sigma A mutants defective in promoter melting.
J Bacteriol: 1994, 176(17);5218-24
[PubMed:8071196] [WorldCat.org] [DOI] (P p)

Y L Juang, J D Helmann
A promoter melting region in the primary sigma factor of Bacillus subtilis. Identification of functionally important aromatic amino acids.
J Mol Biol: 1994, 235(5);1470-88
[PubMed:8107087] [WorldCat.org] [DOI] (P p)

H L Carter, L F Wang, R H Doi, C P Moran
rpoD operon promoter used by sigma H-RNA polymerase in Bacillus subtilis.
J Bacteriol: 1988, 170(4);1617-21
[PubMed:3127379] [WorldCat.org] [DOI] (P p)

C W Price, R H Doi
Genetic mapping of rpoD implicates the major sigma factor of Bacillus subtilis RNA polymerase in sporulation initiation.
Mol Gen Genet: 1985, 201(1);88-95
[PubMed:2997585] [WorldCat.org] [DOI] (P p)

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