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J. Biol. Chem., Vol. 276, Issue 9, 6093-6097, March 2, 2001
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From the Coliphage
The Lysis Protein E of
X174 Is a Specific Inhibitor of the
MraY-catalyzed Step in Peptidoglycan Synthesis*
,¶
Department of Biochemistry and Biophysics,
Texas A&M University and § Department of Medical
Biochemistry and Genetics, Texas A&M University System Health Science
Center, College Station, Texas 77843
X174 encodes a single lysis protein,
E, a 91-amino acid membrane protein. Dominant mutations have been
isolated in the host gene mraY that confer E resistance.
mraY encodes translocase I, which catalyzes the formation
of the first lipid intermediate in bacterial cell wall synthesis,
suggesting a model in which E inhibits MraY and promotes cell lysis in
a manner analogous to cell wall synthesis inhibitors like penicillin.
To test this model biochemically, we monitored the effect of E on cell
wall synthesis in vivo and in vitro. We find
that expression of Emyc, encoding an epitope-tagged E
protein, from a multicopy plasmid inhibits the incorporation of
[3H]diaminopimelic acid into cell wall and leads to a
profile of labeled precursors consistent with MraY inhibition.
Moreover, we find that membranes isolated after Emyc
expression are drastically reduced in MraY activity, whereas the
activity of Rfe, an enzyme in the same superfamily, was unaffected. We
therefore conclude that E is indeed a cell wall synthesis inhibitor and
that this inhibition results from a specific block at the
MraY-catalyzed step in the pathway.
*
This work was supported by United States Public Health
Services Grant GM27099 and by funds from the Robert A. Welch Foundation and the Texas Agricultural Experiment Station.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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