Difference between revisions of "DesK"

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(Original publications)
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<pubmed> 20117042, 17087771</pubmed>
 
==Original publications==
 
==Original publications==
<pubmed>10094672,14734164,12399512,20507988 , 19233289 11285232 19805278 15090506, 12207704 20705470 23356219 </pubmed>
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<pubmed>10094672,14734164,12399512,20507988 , 19233289 11285232 19805278 15090506, 12207704 20705470 23356219 24522108 </pubmed>
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 10:25, 14 February 2014

  • 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
Gene expression levels in SubtiExpress: desK
Interactions involving this protein in SubtInteract: DesK
Metabolic function and regulation of this protein in SubtiPathways:
desK
MW, pI 42 kDa, 9.428
Gene length, protein length 1110 bp, 370 aa
Immediate neighbours des, desR
Sequences Protein DNA DNA_with_flanks
Genetic context
YocF context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
DesK expression.png















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

Database entries

  • KEGG entry: [3]
  • E.C. number:

Additional information

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

Expression and regulation

  • 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

Original publications

María Eugenia Inda, Michel Vandenbranden, Ariel Fernández, Diego de Mendoza, Jean-Marie Ruysschaert, Larisa Estefanía Cybulski
A lipid-mediated conformational switch modulates the thermosensing activity of DesK.
Proc Natl Acad Sci U S A: 2014, 111(9);3579-84
[PubMed:24522108] [WorldCat.org] [DOI] (I p)

Mariana Martín, Diego de Mendoza
Regulation of Bacillus subtilis DesK thermosensor by lipids.
Biochem J: 2013, 451(2);269-75
[PubMed:23356219] [WorldCat.org] [DOI] (I p)

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)