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- W1965722286 abstract "The Bacillus subtilis histidine kinase DesK is a 5 transmembrane stretches- thermosensor suited to remodel membrane fluidity when temperature drops below 30 oC. We have recently designed a hybrid nanosensor with one transmembrane domain which is 5 times smaller than the parental protein. This chimerical protein fully retains, in vivo and in vitro, the sensing properties of the parental system and was called Minimal Sensor-DesK (MS-DesK). A recent paper (1) provides evidence that this perfectly simplified system could serve as a model to study a complex biological phenomena. Thus the MS-DesK is used here to study the conversion of a physical stimulus into a biological response that involves a change in the signaling transduction state.The N-terminus of TMS1 contains three hydrophilic aminoacids near the lipid-water interface creating an instability hot spot. We show that this boundary-sensitive motif controls the sensing and transmission activity by mutagenesis and in vitro reconstitution experiments. Accordingly, we hypothesize that membrane thickness is the temperature agent that determines the signaling state of the cold sensor by dictating the hydration level of the meta-stable hydrophilic spot. Tryptophan-labeled peptides corresponding to the sensor (functional and non-functional) transmembrane domain were synthesized and incorporated into membrane vesicles. Fluorescence spectroscopy and Circular Dichroism data of the peptides incorporated in liposomes of varying fatty acid chain length and different melting temperatures is presented.[1] Cybulski LE, Martin M, Mansilla MC, Fernandez A, de Mendoza D. Membrane thickness cue for cold sensing in a bacterium. Curr Biol. 20: 1539-1544, 2010" @default.
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- W1965722286 date "2012-01-01" @default.
- W1965722286 modified "2023-09-29" @default.
- W1965722286 title "How does Thermosensor Desk Measure Membrane Thickness? Tryptophan Fluorescence and Mutagenesis Analysis" @default.
- W1965722286 doi "https://doi.org/10.1016/j.bpj.2011.11.2705" @default.
- W1965722286 hasPublicationYear "2012" @default.
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