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Expression of extracellular phospholipase from Serratia liquefaciens is growth-phase-dependent, catabolite-repressed and regulated by anaerobiosis
Article first published online: 27 OCT 2006
DOI: 10.1111/j.1365-2958.1992.tb00857.x
1365-2958/asset/cover.gif?v=1&s=75254d9e3ae6a0f08085f34cc6e5bd65d8e3d52e "Molecular Microbiology")
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How to Cite
Givskov, M. and Molin, S. (1992), Expression of extracellular phospholipase from Serratia liquefaciens is growth-phase-dependent, catabolite-repressed and regulated by anaerobiosis. Molecular Microbiology, 6: 1363–1374. doi: 10.1111/j.1365-2958.1992.tb00857.x
Publication History
- Issue published online: 27 OCT 2006
- Article first published online: 27 OCT 2006
- Received 2 December, 1992; revised and accepted 13 February, 1992.
- Abstract
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Summary
Many members of the genus Serratia synthesize and excrete a number of extracellular hydrolytic enzymes. One of these is the phospholipase A1 from Serratia liquefaciens, the expression of which is growth-phase-dependent. Through the use of gene fusions and primer extension analysis we show that the expression of phospholipase is subject to positive transcriptional regulation of a dual promoter system; one promoter positioned approximately 600bp upstream from the phIA gene is responsible for the induction of phospholipase expression under anaerobic conditions, and the other promoter positioned 50bp upstream from the phIA gene is subject to catabolite repression and induced during the transition from exponential to late log-phase of bacterial growth. On the basis of sequence homology and behaviour in the relevant Escherichia coli mutants, we suggest the distant promoter to be Fnr-controlled and the proximal phIA promoter to be a member of the FIbB-controlled flagellar-chemotaxis regulon.