DesR

• Description: two-component response regulator, regulation of cold shock expression of des
  
  

Gene name	desR
Synonyms	yocG
Essential	no
Product	two-component response regulator
Function	regulation of cold shock expression of des
Gene expression levels in SubtiExpress: desR
Interactions involving this protein in SubtInteract: DesR
Metabolic function and regulation of this protein in SubtiPathways: desR
MW, pI	22 kDa, 4.885
Gene length, protein length	597 bp, 199 aa
Immediate neighbours	desK, yocH
Sequences	Protein DNA DNA_with_flanks
Genetic context This image was kindly provided by SubtiList
Expression at a glance   PubMed

Categories containing this gene/protein

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

The DesR regulon:

• des

The gene

Basic information

• Locus tag: BSU19200

Database entries

• BsubCyc: BSU19200

• DBTBS entry: [1]

• SubtiList entry: [2]

The protein

Basic information/ Evolution

• Catalyzed reaction/ biological activity: transcription activation of the des operon when phosphorylated by DesK

• Protein family:

• Paralogous protein(s):

Extended information on the protein

• Kinetic information:

• Domains:

• Modification: phosphorylated by DesK on an Asp residue

• Cofactor(s):

• Effectors of protein activity:

• Interactions:
  • DesK-DesR

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

Database entries

• BsubCyc: BSU19200

• Structure:

• UniProt: O34723

• KEGG entry: [3]

• E.C. number:

Expression and regulation

• Operon: desK-desR PubMed

• Expression browser: desR PubMed

• Sigma factor:

• Regulation:
  • induced by cold shock (18-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

• Diego de Mendoza, Universidad Nacional de Rosario, Argentine homepage

References

Felipe Trajtenberg, Daniela Albanesi, Natalia Ruétalo, Horacio Botti, Ariel E Mechaly, Marcos Nieves, Pablo S Aguilar, Larisa Cybulski, Nicole Larrieux, Diego de Mendoza, Alejandro Buschiazzo
Allosteric activation of bacterial response regulators: the role of the cognate histidine kinase beyond phosphorylation.
mBio: 2014, 5(6);e02105
[PubMed:25406381] [WorldCat.org] [DOI] (I e)

Sebastián R Najle, María E Inda, Diego de Mendoza, Larisa E Cybulski
Oligomerization of Bacillus subtilis DesR is required for fine tuning regulation of membrane fluidity.
Biochim Biophys Acta: 2009, 1790(10);1238-43
[PubMed:19595746] [WorldCat.org] [DOI] (P 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)

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)