Archives of Microbiology

, Volume 183, Issue 4, pp 229–235

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

Mini-Review

DOI: 10.1007/s00203-005-0759-8

Cite this article as:
Mansilla, M.C. & de Mendoza, D. Arch Microbiol (2005) 183: 229. doi:10.1007/s00203-005-0759-8
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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.

Keywords

Regulation of membrane lipid synthesisDesaturase topologySignal transduction

Copyright information

© Springer-Verlag 2005

Authors and Affiliations

  1. 1.Departamento de Microbiología, Facultad de Ciencias Bioquímicas y Farmacéuticas, Instituto de Biología Molecular y Celular de Rosario (IBR)Universidad Nacional de RosarioRosarioArgentina