Bacillus subtilis DesR functions as a phosphorylation-activated switch to control membrane lipid fluidity.

被引:63
作者
Cybulski, LE
del Solar, G
Craig, PO
Espinosa, M
de Mendoza, D
机构
[1] Univ Nacl Rosario, Consejo Nacl Invest Cient & Tecn, Inst Biol Mol & Celular Rosario, RA-2000 Rosario, Santa Fe, Argentina
[2] Univ Nacl Rosario, Fac Ciencias Bioquim & Farmaceut, Dept Microbiol, RA-2000 Rosario, Santa Fe, Argentina
[3] CSIC, Ctr Invest Biol, Madrid 28040, Spain
[4] Inst Leloir, Buenos Aires, DF, Argentina
关键词
D O I
10.1074/jbc.M405150200
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The Des pathway of Bacillus subtilis regulates the synthesis of the cold-shock induced membrane-bound enzyme Delta5-fatty acid desaturase (Delta5-Des). A central component of the Des pathway is the response regulator, DesR, which is activated by a membrane-associated kinase, DesK, in response to a decrease in membrane lipid fluidity. Despite genetic and biochemical studies, specific details of the interaction between DesR and the DNA remain unknown. In this study we show that only the phosphorylated form of protein DesR is able to bind to a regulatory region immediately upstream of the promoter of the Delta5-Des gene (Pdes). Phosphorylation of the regulatory domain of dimeric DesR promotes, in a cooperative fashion, the hierarchical occupation of two adjacent, non-identical, DesR-P DNA binding sites, so that there is a shift in the equilibrium toward the tetrameric active form of the response regulator. Subsequently, this phosphorylation signal propagation leads to the activation of the des gene through recruitment of RNA polymerase to Pdes. This is the first dissected example of a transcription factor functioning as a phosphorylation-activated switch for a cold-shock gene, allowing the cell to optimize the fluidity of membrane phospholipids.
引用
收藏
页码:39340 / 39347
页数:8
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共 37 条
  • [1] Transcriptional control of the low-temperature-inducible des gene, encoding the Δ5 desaturase of Bacillus subtilis
    Aguilar, PS
    Lopez, P
    De Mendoza, D
    [J]. JOURNAL OF BACTERIOLOGY, 1999, 181 (22) : 7028 - 7033
  • [2] A Bacillus subtilis gene induced by cold shock encodes a membrane phospholipid desaturase
    Aguilar, PS
    Cronan, JE
    de Mendoza, D
    [J]. JOURNAL OF BACTERIOLOGY, 1998, 180 (08) : 2194 - 2200
  • [3] Molecular basis of thermosensing:: a two-component signal transduction thermometer in Bacillus subtilis
    Aguilar, PS
    Hernandez-Arriaga, AM
    Cybulski, LE
    Erazo, AC
    de Mendoza, D
    [J]. EMBO JOURNAL, 2001, 20 (07) : 1681 - 1691
  • [4] The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator
    Albanesi, D
    Mansilla, MC
    de Mendoza, D
    [J]. JOURNAL OF BACTERIOLOGY, 2004, 186 (09) : 2655 - 2663
  • [5] The Bacillus subtilis acyl lipid desaturase is a Δ5 desaturase
    Altabe, SG
    Aguilar, P
    Caballero, GM
    de Mendoza, D
    [J]. JOURNAL OF BACTERIOLOGY, 2003, 185 (10) : 3228 - 3231
  • [6] Structure of the Escherichia coli response regulator NarL
    Baikalov, I
    Schroder, I
    KaczorGrzeskowiak, M
    Grzeskowiak, K
    Gunsalus, RP
    Dickerson, RE
    [J]. BIOCHEMISTRY, 1996, 35 (34) : 11053 - 11061
  • [7] SIGNAL TRANSDUCTION PATHWAYS INVOLVING PROTEIN-PHOSPHORYLATION IN PROKARYOTES
    BOURRET, RB
    BORKOVICH, KA
    SIMON, MI
    [J]. ANNUAL REVIEW OF BIOCHEMISTRY, 1991, 60 : 401 - 441
  • [8] The regulation of bacterial transcription initiation
    Browning, DF
    Busby, SJW
    [J]. NATURE REVIEWS MICROBIOLOGY, 2004, 2 (01) : 57 - 65
  • [9] Mechanism of membrane fluidityoptimization:: isothermal control of the Bacillus subtilis acyl-lipid desaturase
    Cybulski, LE
    Albanesi, D
    Mansilla, MC
    Altabe, S
    Aguilar, PS
    de Mendoza, D
    [J]. MOLECULAR MICROBIOLOGY, 2002, 45 (05) : 1379 - 1388
  • [10] Phosphorylation-induced dimerization of the FixJ receiver domain
    Da Re, S
    Schumacher, J
    Rousseau, P
    Fourment, J
    Ebel, C
    Kahn, D
    [J]. MOLECULAR MICROBIOLOGY, 1999, 34 (03) : 504 - 511