Difference between revisions of "Des"

From SubtiWiki
Jump to: navigation, search
(References)
Line 16: Line 16:
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU19180 des]
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Gene expression levels in [http://subtiwiki.uni-goettingen.de/apps/expression/ ''Subti''Express]''': [http://subtiwiki.uni-goettingen.de/apps/expression/expression.php?search=BSU19180 des]
 
|-
 
|-
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://cellpublisher.gobics.de/subtinteract/startpage/start/ ''Subt''Interact]''': [http://cellpublisher.gobics.de/subtinteract/interactionList/2/Des Des]
+
|colspan="2" style="background:#FAF8CC;" align="center"| '''Interactions involving this protein in [http://subtiwiki.uni-goettingen.de/interact/ ''Subt''Interact]''': [http://subtiwiki.uni-goettingen.de/interact/index.php?protein=Des Des]
 
|-
 
|-
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_deg.html Fatty acid degradation]'''
 
|colspan="2" style="background:#FAF8CC;" align="center"| '''Metabolic function and regulation of this protein in [[SubtiPathways|''Subti''Pathways]]: <br/>[http://subtiwiki.uni-goettingen.de/pathways/fatty_acid_deg.html Fatty acid degradation]'''

Revision as of 08:35, 12 November 2013

  • Description: phospholipid desaturase

Gene name des
Synonyms yocE
Essential no
Product phospholipid desaturase
Function adaptation of membrane fluidity at low temperatures
Gene expression levels in SubtiExpress: des
Interactions involving this protein in SubtInteract: Des
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
Sequences Protein DNA DNA_with_flanks
Genetic context
Des context.gif
This image was kindly provided by SubtiList
Expression at a glance   PubMed
Des expression.png




























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

Database entries

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

Additional information

    • in strains evolved for growth at low pressure, des expression is significantly increased as compared to the wild type, this allows growth at low pressure PubMed

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:

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:
    • in strains evolved for growth at low pressure, des expression is significantly increased as compared to the wild type PubMed

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

Patricia Fajardo-Cavazos, Samantha M Waters, Andrew C Schuerger, Sheeja George, James J Marois, Wayne L Nicholson
Evolution of Bacillus subtilis to enhanced growth at low pressure: up-regulated transcription of des-desKR, encoding the fatty acid desaturase system.
Astrobiology: 2012, 12(3);258-70
[PubMed:22416764] [WorldCat.org] [DOI] (I p)

Lorena Chazarreta-Cifre, Leticia Martiarena, Diego de Mendoza, Silvia G Altabe
Role of ferredoxin and flavodoxins in Bacillus subtilis fatty acid desaturation.
J Bacteriol: 2011, 193(16);4043-8
[PubMed:21665975] [WorldCat.org] [DOI] (I p)

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)

Jana Beranová, Małgorzata Jemioła-Rzemińska, Dana Elhottová, Kazimierz Strzałka, Ivo Konopásek
Metabolic control of the membrane fluidity in Bacillus subtilis during cold adaptation.
Biochim Biophys Acta: 2008, 1778(2);445-53
[PubMed:18154726] [WorldCat.org] [DOI] (P 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)