A Thermolabile Repression System

  1. Tadao Horiuchi and
  2. Aaron Novick
  1. Institute of Molecular Biology, University of Oregon, Eugene, Oregon

This extract was created in the absence of an abstract.

Excerpt

We have isolated an E. coli mutant in which the regulatory system controlling the synthesis of β-galactosidase has become thermolabile (Horiuchi, Horiuchi and Novick, 1961). This mutant, called E103, is derived from E102, a methionine-requiring Cavalli Hfr strain (Horiuchi, Tomizawa, and Novick, 1961).

At lower temperatures the mutant is like the wild-type strain in being inducible, i.e., a specific inducer is required for the synthesis of β-galactosidase. At higher temperatures it resembles a constitutive mutant, i.e., β-galactosidase is made at high rates independent of the presence of inducer. For example, β-galactosidase is made by E103 at 14° at 0.5% of maximum rate and at 43.5° at about 40% of maximum. In comparison, this enzyme is made by the wild type (E10.2) at about 0.1% of maximum at both temperatures. In the presence of inducer, both E103 and E102 make β-galactosidase at full rate at both temperatures. Also, a typical constitutive...

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    * On leave from the National Institute of Health of Japan, Tokyo, Japan.

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