a Departamento de Biologia Celular, Facultad de Ciencias, Universidad Central de Venezuela, Caracas, Venezuela
ABSTRACT
A spontaneously arising regulatory mutant of the gluconate system in Escherichia coli was isolated. This mutant became constitutive, probably in one step, for gluconate high-affinity transport, gluconokinase, and gluconate-6-P dehydrase. The mutation involved (gntR18) is cotransducible with asd. Pseudorevertants, derived from a mutant (M2) that shows a long lag for growth on gluconate mineral medium, were also isolated and characterized. They give constitutive levels of gluconokinase and gluconate-6-P dehydrase but lack high-affinity transport function. Genetic experiments performed with one of these pseudorevertants (M4) indicate that it carries a secondary mutation in the gntR gene. The M4 phenotype is thus the result of the interaction of expression of a constitutive mutation (gntR4) with the mutation of strain M2 (gntM2).
1 Present address: Departamento de Biologia, Fundoción Bariloche, Casilla de Correo 138, Bariloche, Argentina.
2 Present address: Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Mass. 02115.
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