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J. Biol. Chem., Vol. 280, Issue 19, 18689-18695, May 13, 2005

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Identification of Multiple Genes Encoding Membrane Proteins with Undecaprenyl Pyrophosphate Phosphatase (UppP) Activity in Escherichia coli^*

Meriem El Ghachi, Anne Derbise, Ahmed Bouhss, and Dominique Mengin-Lecreulx¶

From the Laboratoire des Enveloppes Bactériennes et Antibiotiques, Unite Mixte de Recherche 8619 CNRS, Université Paris-Sud, 91405 Orsay, France

The bacA gene product of Escherichia coli was recently purified to near homogeneity and identified as an undecaprenyl pyrophosphate phosphatase activity (El Ghachi, M., Bouhss, A., Blanot, D., and Mengin-Lecreulx, D. (2004) J. Biol. Chem. 279, 30106–30113). The enzyme function is to synthesize the carrier lipid undecaprenyl phosphate that is essential for the biosynthesis of peptidoglycan and other cell wall components. The inactivation of the chromosomal bacA gene was not lethal but led to a significant, but not total, depletion of undecaprenyl pyrophosphate phosphatase activity in E. coli membranes, suggesting that other(s) protein(s) should exist and account for the residual activity and viability of the mutant strain. Here we report that inactivation of two additional genes, ybjG and pgpB, is required to abolish growth of the bacA mutant strain. Overexpression of either of these genes, or of a fourth identified one, yeiU, is shown to result in bacitracin resistance and increased levels of undecaprenyl pyrophosphate phosphatase activity, as previously observed for bacA. A thermosensitive conditional triple mutant bacA,ybjG,pgpB in which the expression of bacA is impaired at 42 °C was constructed. This strain was shown to accumulate soluble peptidoglycan nucleotide precursors and to lyse when grown at the restrictive temperature, due to the depletion of the pool of undecaprenyl phosphate and consequent arrest of cell wall synthesis. This work provides evidence that two different classes of proteins exhibit undecaprenyl pyrophosphate phosphatase activity in E. coli and probably other bacterial species; they are the BacA enzyme and several members from a superfamily of phosphatases that, different from BacA, share in common a characteristic phosphatase sequence motif.

Received for publication, October 29, 2004 , and in revised form, February 14, 2005.

^* This work was supported in part by grants from the European Community (FP6, LSHM-CT-2003-503335, "COBRA" project) and from the Centre National de la Recherche Scientifique (UMR 8619). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Recipient of a scholarship from the Ministère de l'Education Nationale, de la Recherche et de la Technologie (Ecole Doctorale "Innovation Thérapeutique, du Fondamental à l'Appliqué").

Supported by Hoechst Marion Roussel AG. Present address: Unité des Yersinia, Institut Pasteur, 28 Rue du Dr. Roux, 75724 Paris Cedex 15, France.

^¶ To whom correspondence should be addressed: Laboratoire des Enveloppes Bactériennes et Antibiotiques, Institut de Biochimie et Biophysique Moléculaire et Cellulaire, UMR 8619 CNRS, Université Paris-Sud, Btiment 430, 91405 Orsay Cedex, France. Tel.: 33-1-69-15-48-41; Fax: 33-1-69-85-37-15; E-mail: dominique.mengin-lecreulx{at}ebp.u-psud.fr.

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