Difference between revisions of "SigA"

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(References)
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=References=
 
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<pubmed> 19680289  20817769 ,2997585,9658000,3127379,10438769,11535782,7599136, 9144176</pubmed>
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<pubmed> 19680289  20817769 ,2997585,9658000,3127379,</pubmed>
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<pubmed>, 10438769,11535782,7599136, 9144176</pubmed>
  
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<pubmed> 12486038,10556308,8107087, 14762002,7918363,8071196,7630711,9185571,9287022, 14679239, 14976210 19735077, </pubmed>
 
<pubmed> 12486038,10556308,8107087, 14762002,7918363,8071196,7630711,9185571,9287022, 14679239, 14976210 19735077, </pubmed>
  
<pubmed> 20935043</pubmed>
 
 
Additional publication: {{PubMed|20935043}}
 
Additional publication: {{PubMed|20935043}}
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:23, 17 October 2010

Gene name sigA
Synonyms rpoD, crsA
Essential yes PubMed
Product RNA polymerase major sigma factor SigA
Function transcription
MW, pI 42 kDa, 4.634
Gene length, protein length 1113 bp, 371 aa
Immediate neighbours cccA, antE
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
SigA context.gif
This image was kindly provided by SubtiList





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:
  • Localization: cell membrane (according to Swiss-Prot)

Database entries

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

Additional information

Expression and regulation

  • Regulation:
  • 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

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)

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)

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)

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)


2

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)

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)

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)

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)

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)

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)


Additional publication: PubMed