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Mol Gen Genet. 1980 Apr;178(1):155-64.

Serine sensitivity of Escherichia coli K 12: partial characterization of a serine resistnat mutant that is extremely sensitive to 2-ketobutyrate.

Abstract

E. coli wild type bacteria display sensitivity towards serine. A selection medium is described which allows selection of serine resistant mutants. One such mutant is described which presents pleiotropic alterations: it exhibits a thermosensitive growth pattern, alteration in the metabolism of the pppGpp and ppGpp nucleotides, cAMP intracellular level alteration, extreme sensitivity to 2-ketobutyric acid and a defect in the phosphotransferases permeation system. A conjecture explaining these apparently unrelated defects supposes that serine metabolism interferes via phosphoenol pyruvate with a cytoplasmic control of membrane activity (the mutant would be defective in the coupling between membrane and the protein responsible for its cytoplasmic control) and that 2-ketobutyrate is an effector of this activity.

PMID:
6247616
[Indexed for MEDLINE]

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