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Journal of Bacteriology, August 1998, p. 4291-4293, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Substitution of an Alanine Residue for Glycine 146 in TMP Kinase from Escherichia coli Is Responsible for Bacterial Hypersensitivity to Bromodeoxyuridine

Lise Tourneux,1 Nadia Bucurenci,1,dagger Ioan Lascu,2 Hiroshi Sakamoto,1 Gilbert Briand,3 and Anne-Marie Gilles1,*

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

Received 15 April 1998/Accepted 12 June 1998

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.

* Corresponding author. Mailing address: Laboratoire de Chimie Structurale des Macromolécules, Institut Pasteur, 28, rue du Docteur Roux, 75724 Paris Cedex 15, France. Phone: 33 (1) 45 68 89 68. Fax: 33 (1) 45 68 84 05. E-mail: amgilles{at}pasteur.fr.

dagger Present address: Institute Cantacuzino, 70100 Bucharest, Romania.

Journal of Bacteriology, August 1998, p. 4291-4293, Vol. 180, No. 16
0021-9193/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

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