Difference between revisions of "DesK"

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= [[Categories]] containing this gene/protein =
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{{SubtiWiki category|[[lipid metabolism/ other]]}},
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{{SubtiWiki category|[[protein modification]]}},
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{{SubtiWiki category|[[transcription factors and their control]]}},
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{{SubtiWiki category|[[cold stress proteins]]}},
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{{SubtiWiki category|[[membrane proteins]]}},
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{{SubtiWiki category|[[phosphoproteins]]}}
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= This gene is a member of the following [[regulons]] =
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=The gene=
 
=The gene=
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= Categories containing this gene/protein =
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{{SubtiWiki category|[[lipid metabolism/ other]]}},
 
{{SubtiWiki category|[[protein modification]]}},
 
{{SubtiWiki category|[[transcription factors and their control]]}},
 
{{SubtiWiki category|[[cold stress proteins]]}},
 
{{SubtiWiki category|[[membrane proteins]]}},
 
{{SubtiWiki category|[[phosphoproteins]]}}
 
 
=The protein=
 
=The protein=
  

Revision as of 20:20, 8 December 2010

  • Description: two-component sensor kinase, regulation of cold shock expression of des

Gene name desK
Synonyms yocF
Essential no
Product two-component sensor kinase
Function regulation of cold shock expression of des
Metabolic function and regulation of this protein in SubtiPathways:
Fatty acid degradation
MW, pI 42 kDa, 9.428
Gene length, protein length 1110 bp, 370 aa
Immediate neighbours des, desR
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
YocF context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

lipid metabolism/ other, protein modification, transcription factors and their control, cold stress proteins, membrane proteins, phosphoproteins

This gene is a member of the following regulons

The gene

Basic information

  • Locus tag: BSU19190

Phenotypes of a mutant

Database entries

  • DBTBS entry: [1]
  • SubtiList entry: [2]

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: autophosphorylation, phosphorylation of DesR
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
    • 5 transmembrane helices
    • cytoplasmatic C-terminal trail
  • Modification: autophosphorylation on a His residue
  • Cofactor(s):
  • Effectors of protein activity: unsaturated fatty acids are negative effectors of the system
  • Localization: membrane (transmembrane segments)

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

  • DesK has the ability to sense changes in membrane fluidity PubMed

Expression and regulation

  • Sigma factor:
  • Regulation:
    • induced by cold shock (12-fold) PubMed
  • 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

Reviews

Richard C Stewart
Protein histidine kinases: assembly of active sites and their regulation in signaling pathways.
Curr Opin Microbiol: 2010, 13(2);133-41
[PubMed:20117042] [WorldCat.org] [DOI] (I p)

Pablo S Aguilar, Diego de Mendoza
Control of fatty acid desaturation: a mechanism conserved from bacteria to humans.
Mol Microbiol: 2006, 62(6);1507-14
[PubMed:17087771] [WorldCat.org] [DOI] (P p)

Original publications

Larisa E Cybulski, Mariana Martín, María C Mansilla, Ariel Fernández, Diego de Mendoza
Membrane thickness cue for cold sensing in a bacterium.
Curr Biol: 2010, 20(17);1539-44
[PubMed:20705470] [WorldCat.org] [DOI] (I p)

Felipe Trajtenberg, Martin Graña, Natalia Ruétalo, Horacio Botti, Alejandro Buschiazzo
Structural and enzymatic insights into the ATP binding and autophosphorylation mechanism of a sensor histidine kinase.
J Biol Chem: 2010, 285(32);24892-903
[PubMed:20507988] [WorldCat.org] [DOI] (I p)

Daniela Albanesi, Mariana Martín, Felipe Trajtenberg, María C Mansilla, Ahmed Haouz, Pedro M Alzari, Diego de Mendoza, Alejandro Buschiazzo
Structural plasticity and catalysis regulation of a thermosensor histidine kinase.
Proc Natl Acad Sci U S A: 2009, 106(38);16185-90
[PubMed:19805278] [WorldCat.org] [DOI] (I p)

Mariana Martín, Daniela Albanesi, Pedro M Alzari, Diego de Mendoza
Functional in vitro assembly of the integral membrane bacterial thermosensor DesK.
Protein Expr Purif: 2009, 66(1);39-45
[PubMed:19233289] [WorldCat.org] [DOI] (I p)

Daniela Albanesi, María Cecilia Mansilla, Diego de Mendoza
The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator.
J Bacteriol: 2004, 186(9);2655-63
[PubMed:15090506] [WorldCat.org] [DOI] (P p)

Karen Hunger, Carsten L Beckering, Mohamed A Marahiel
Genetic evidence for the temperature-sensing ability of the membrane domain of the Bacillus subtilis histidine kinase DesK.
FEMS Microbiol Lett: 2004, 230(1);41-6
[PubMed:14734164] [WorldCat.org] [DOI] (P p)

Carsten L Beckering, Leif Steil, Michael H W Weber, Uwe Völker, Mohamed A Marahiel
Genomewide transcriptional analysis of the cold shock response in Bacillus subtilis.
J Bacteriol: 2002, 184(22);6395-402
[PubMed:12399512] [WorldCat.org] [DOI] (P p)

Larisa E Cybulski, Daniela Albanesi, María C Mansilla, Silvia Altabe, Pablo S Aguilar, Diego de Mendoza
Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase.
Mol Microbiol: 2002, 45(5);1379-88
[PubMed:12207704] [WorldCat.org] [DOI] (P p)

P S Aguilar, A M Hernandez-Arriaga, L E Cybulski, A C Erazo, D de Mendoza
Molecular basis of thermosensing: a two-component signal transduction thermometer in Bacillus subtilis.
EMBO J: 2001, 20(7);1681-91
[PubMed:11285232] [WorldCat.org] [DOI] (P p)

C Fabret, V A Feher, J A Hoch
Two-component signal transduction in Bacillus subtilis: how one organism sees its world.
J Bacteriol: 1999, 181(7);1975-83
[PubMed:10094672] [WorldCat.org] [DOI] (P p)