Substitution of an Alanine Residue for Glycine 146 in TMP Kinase from Escherichia coli Is Responsible for Bacterial Hypersensitivity to Bromodeoxyuridine |
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| Authors: | Lise Tourneux Nadia Bucurenci Ioan Lascu Hiroshi Sakamoto Gilbert Briand and Anne-Marie Gilles |
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| Institution: | Laboratoire de Chimie Structurale des Macromolécules, Institut Pasteur, 75724 Paris Cedex 15,1. Institut de Biochimie et Génétique Cellulaires, Université de Bordeaux II, 33077 Bordeaux Cedex,2. and Laboratoire d’Application de Spectrométrie de Masse, Université de Lille II, 59045 Lille Cedex,3. France |
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| Abstract: | The wild-type TMP kinases from Escherichia coli and from a strain hypersensitive to 5-bromo-2′-deoxyuridine were characterized comparatively. The mutation at codon 146 causes the substitution of an alanine residue for glycine in the enzyme, which is accompanied by changes in the relative affinities for 5-Br-UMP and TMP compared to those of the wild-type TMP kinase. Plasmids carrying the wild-type tmk gene from Escherichia coli or Bacillus subtilis, but not the defective tmk gene, restored the resistance to bromodeoxyuridine of an E. coli mutant strain. |
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