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A more recent version of this article appeared on May 13, 2005
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M412277200v1
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Papers In Press, published online ahead of print March 18, 2005
J. Biol. Chem, 10.1074/jbc.M412277200
Submitted on October 29, 2004
Revised on February 14, 2005
Accepted on March 18, 2005

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

Departimente di Biochemie, Universite Paris-Sud, Orsay 91405

Corresponding Author: dominique.mengin-lecreulx{at}ebp.u-psud.fr

The bacA gene product of Escherichia coli was recently purified to near homogeneity and identified as an undecaprenyl pyrophosphate phosphatase (UppP) activity (M. El Ghachi, A. Bouhss, D. Blanot, and D. Mengin-Lecreulx, 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: the BacA enzyme and several members from a super-family of phosphatases which, to the difference of BacA, share in common a characteristic phosphatase sequence motif.


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