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. 1967 Jul;94(1):87–91. doi: 10.1128/jb.94.1.87-91.1967

Derepression of Alkaline Phosphatase in Escherichia coli by p-Fluorophenylalanine

Soosang Kang 1, Alvin Markovitz 1
PMCID: PMC251875  PMID: 5338975

Abstract

p-Fluorophenylalanine (FPA) causes a 100-fold increase in alkaline phosphatase in Escherichia coli B, strain PR1 at 30 C in minimal medium that contains excess inorganic phosphate (1.92 × 10−3m). Little increase in alkaline phosphatase synthesis occurs under these conditions at 22 C. [This strain is known to have a mutation in a regulator gene (R2) that, in the absence of FPA, permits derepression of alkaline phosphatase synthesis at 37 C, but not at 30 C or below.] In contrast, E. coli B3 (the strain from which E. coli B strain PR1 was derived) is not derepressed at 30 C by FPA. 14C-FPA is incorporated into bacterial proteins. Temperature-shift experiments (30 C⇌22 C) in the presence of FPA are consistent with the following mechanism. FPA is incorporated into the genetically altered R2 protein at 30 and 22 C. This further alteration due to the incorporation of analogue makes the R2 protein inactive at 30 C, but active at 22 C.

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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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