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The Bacillus subtilis desaturase: a model to understand phospholipid modification and temperature sensing

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Abstract

Most fatty acid desaturases are members of a large superfamily of integral membrane, O2-dependent, iron-containing enzymes that insert double bonds into previously synthesized fatty acyl chains. The cold shock-induced, membrane-bound desaturase from Bacillus subtilis (Δ5-Des) uses existing phospholipids as substrates to introduce a cis-double bond at the fifth position of the fatty acyl chain. While essentially no three-dimensional structural information is available for these difficult-to-purify enzymes, experimental analysis of the topology of Δ5-Des has provided a model that might be extended to most acyl-lipid desaturases. In addition, studies of the cold-induced expression of Δ5-Des led to the identification of a two-component system composed of a membrane-associated kinase, DesK, and a transcriptional regulator, DesR, which stringently controls the transcription of the des gene, coding for the desaturase. A model for sensing and transduction of low-temperature signals has emerged from our results, which we discuss in the context of transcriptional regulation of membrane lipid fluidity homeostasis.

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Acknowledgements

This work was supported by a grant from Agencia Nacional de Promoción Científica y Tecnológica (FONCYT). M.C. Mansilla and D. de Mendoza are Career Investigators from Consejo Nacional de Investigaciones Científicas y Técnicas (CONICET). D. de Mendoza is an International Research Scholar from Howard Hughes Medical Institute.

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Correspondence to Diego de Mendoza.

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Mansilla, M.C., de Mendoza, D. The Bacillus subtilis desaturase: a model to understand phospholipid modification and temperature sensing. Arch Microbiol 183, 229–235 (2005). https://doi.org/10.1007/s00203-005-0759-8

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  • DOI: https://doi.org/10.1007/s00203-005-0759-8

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