This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Kang, S. Articles by Markovitz, A. Search for Related Content PubMed PubMed Citation Articles by Kang, S. Articles by Markovitz, A.

Derepression of Alkaline Phosphatase in Escherichia coli by p-Fluorophenylalanine

Department of Microbiology and La Rabida-University of Chicago Institute, University of Chicago, Chicago, Illinois 60637

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 x 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 C22 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.

This article has been cited by other articles:

• Goldman, P. (1969). The Carbon-Fluorine Bond in Compounds of Biological Interest. Science 164: 1123-1130