Bacillus subtilis DesR functions as a phosphorylation-activated switch to control membrane lipid fluidity (Q47215460)

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title

Bacillus subtilis DesR functions as a phosphorylation-activated switch to control membrane lipid fluidity (English)

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author name string

Larisa E Cybulski

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Patricio O Craig

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Manuel Espinosa

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Diego de Mendoza

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language of work or name

English

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publication date

9 July 2004

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Journal of Biological Chemistry

published in

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volume

279

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issue

38

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page(s)

39340-39347

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Two-component and phosphorelay signal transduction

cites work

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Two-component signal transduction

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The Bacillus subtilis acyl lipid desaturase is a delta5 desaturase.

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Mechanism of membrane fluidity optimization: isothermal control of the Bacillus subtilis acyl-lipid desaturase

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The membrane fluidity sensor DesK of Bacillus subtilis controls the signal decay of its cognate response regulator

21 January 2018

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Activation of the yeast SSK2 MAP kinase kinase kinase by the SSK1 two-component response regulator

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Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension

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Bacillus subtilis PhoP binds to the phoB tandem promoter exclusively within the phosphate starvation-inducible promoter

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Multimerization of phosphorylated and non-phosphorylated ArcA is necessary for the response regulator function of the Arc two-component signal transduction system

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Transcriptional and post-transcriptional control of cold-shock genes

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Dimerization allows DNA target site recognition by the NarL response regulator

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Identifiers

DOI

10.1074/JBC.M405150200

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