Difference between revisions of "Des"

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= [[Categories]] containing this gene/protein =
 
= [[Categories]] containing this gene/protein =
 
{{SubtiWiki category|[[lipid metabolism/ other]]}},
 
{{SubtiWiki category|[[lipid metabolism/ other]]}},
{{SubtiWiki category|[[cold stress proteins]]}}
+
{{SubtiWiki category|[[cold stress proteins]]}},
 +
{{SubtiWiki category|[[membrane proteins]]}}
  
 
= This gene is a member of the following [[regulons]] =
 
= This gene is a member of the following [[regulons]] =
Line 135: Line 136:
  
 
=References=
 
=References=
<pubmed>19164152,11251847,12399512,9555904 10559169 11285232 , 12207704 12730185 19820084 12207704 20581210 21665975 </pubmed>
+
<pubmed>19164152,11251847,12399512,9555904 10559169 11285232 , 12207704 12730185 19820084 12207704 20581210 </pubmed>
 
==Additional papers==
 
==Additional papers==
{{PubMed|18154726}}
+
{{PubMed|18154726,21665975}}
 
[[Category:Protein-coding genes]]
 
[[Category:Protein-coding genes]]

Revision as of 16:56, 1 July 2011

  • Description: phospholipid desaturase

Gene name des
Synonyms yocE
Essential no
Product phospholipid desaturase
Function adaptation of membrane fluidity at low temperatures
Metabolic function and regulation of this protein in SubtiPathways:
Fatty acid degradation
MW, pI 40 kDa, 9.88
Gene length, protein length 1056 bp, 352 aa
Immediate neighbours yocD, desK
Get the DNA and protein sequences
(Barbe et al., 2009)
Genetic context
Des context.gif
This image was kindly provided by SubtiList







Categories containing this gene/protein

lipid metabolism/ other, cold stress proteins, membrane proteins

This gene is a member of the following regulons

DesR regulon

The gene

Basic information

  • Locus tag: BSU19180

Phenotypes of a mutant

cold-sensitive PubMed

Database entries

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

Additional information

The protein

Basic information/ Evolution

  • Catalyzed reaction/ biological activity: introduces double bonds into long chain fatty acids PubMed
  • Protein family:
  • Paralogous protein(s):

Extended information on the protein

  • Kinetic information:
  • Domains:
  • Modification:
  • Cofactor(s):
    • Des receives electrons from ferredoxin (Fer) or from either of the two flavodoxins, YkuN or YkuP, the three proteins can functionally replace each other PubMed
  • Effectors of protein activity:
  • Localization: integral membrane protein PubMed

Database entries

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

Additional information

Expression and regulation

  • Regulation:
    • induced upon cold shock (DesR) PubMed
    • repressed at increased membrane fluidity PubMed
  • 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

Jana Beranová, María C Mansilla, Diego de Mendoza, Dana Elhottová, Ivo Konopásek
Differences in cold adaptation of Bacillus subtilis under anaerobic and aerobic conditions.
J Bacteriol: 2010, 192(16);4164-71
[PubMed:20581210] [WorldCat.org] [DOI] (I p)

Natalia Martin, Esteban Lombardía, Silvia G Altabe, Diego de Mendoza, María C Mansilla
A lipA (yutB) mutant, encoding lipoic acid synthase, provides insight into the interplay between branched-chain and unsaturated fatty acid biosynthesis in Bacillus subtilis.
J Bacteriol: 2009, 191(24);7447-55
[PubMed:19820084] [WorldCat.org] [DOI] (I p)

Anna-Barbara Hachmann, Esther R Angert, John D Helmann
Genetic analysis of factors affecting susceptibility of Bacillus subtilis to daptomycin.
Antimicrob Agents Chemother: 2009, 53(4);1598-609
[PubMed:19164152] [WorldCat.org] [DOI] (I p)

Silvia G Altabe, Pablo Aguilar, Gerardo M Caballero, Diego de Mendoza
The Bacillus subtilis acyl lipid desaturase is a delta5 desaturase.
J Bacteriol: 2003, 185(10);3228-31
[PubMed:12730185] [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)

M H Weber, W Klein, L Müller, U M Niess, M A Marahiel
Role of the Bacillus subtilis fatty acid desaturase in membrane adaptation during cold shock.
Mol Microbiol: 2001, 39(5);1321-9
[PubMed:11251847] [WorldCat.org] [DOI] (P p)

P S Aguilar, P Lopez, D de Mendoza
Transcriptional control of the low-temperature-inducible des gene, encoding the delta5 desaturase of Bacillus subtilis.
J Bacteriol: 1999, 181(22);7028-33
[PubMed:10559169] [WorldCat.org] [DOI] (P p)

P S Aguilar, J E Cronan, D de Mendoza
A Bacillus subtilis gene induced by cold shock encodes a membrane phospholipid desaturase.
J Bacteriol: 1998, 180(8);2194-200
[PubMed:9555904] [WorldCat.org] [DOI] (P p)

Additional papers

PubMed