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. 1976 Nov;128(2):522–527. doi: 10.1128/jb.128.2.522-527.1976

Enzyme secretion in Escherichia coli: synthesis of alkaline phosphatase and acid hexose phosphatase in the absence of phospholipid synthesis.

I R Beacham, N S Taylor, M Youell
PMCID: PMC232786  PMID: 789356

Abstract

De novo synthesis of two periplasmic enzymes in Escherichia coli, alkaline phosphatase and acid hexose phosphatase, have been studied in the presence and absence of new phospholipid synthesis. Alkaline phosphatase synthesis was initiated by a temperature shift in a strain carrying a phoA amber mutation and a temperature-sensitive suppressor mutation; acid hexose phosphatase was studied after relief of catabolite repression. Glycerol auxotrophs (gpsA) were used to control phospholipid synthesis. Synthesis of both enzymes proceeded at a normal rate for 0.5 to 1.0 generation of growth, although it was then curtailed. It is concluded that secretion of these enzymes is not obligatorily coupled to new net phospholipid synthesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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