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J. Biol. Chem., Vol. 267, Issue 17, 11806-11810, 06, 1992
MK Rumley, H Therisod, AC Weissborn and EP Kennedy
The periplasmic glucans of Gram-negative bacteria, including the
membrane-derived oligosaccharides (MDO) of Escherichia coli and the cyclic
glucans of the Rhizobiaceae, have important but poorly understood functions
in osmotic adaptation and, in the case of the Rhizobiaceae, in the complex
cell-signaling of these bacteria with specific plant hosts. Experiments on
the mechanisms of osmotic regulation of the biosynthesis of MDO in E. coli
reported here support a model in which osmotic regulation occurs
principally at the level of modulation of enzyme activity rather than at
the level of gene expression. 1) Activity of the membrane-bound
glucosyltransferase thought to catalyze the first and rate-making step in
the biosynthesis of MDO is not altered by the osmolarity of the medium in
which cells are grown. 2) Upon dilution of cells growing at high osmolarity
into a medium of low osmolarity, the increased synthesis of MDO begins at
maximum rate without detectable lag. 3) The activity of the membrane
glucosyltransferase in vitro is strongly inhibited by high levels of salts,
consistent with the view that synthesis in vivo is regulated chiefly by
this mechanism, rather than by regulation of the synthesis of biosynthetic
enzymes. We also find that the biosynthesis of MDO is regulated not only
osmotically but also by strong feedback inhibition in response to the
levels of MDO in the periplasm.
Mechanisms of regulation of the biosynthesis of membrane-derived oligosaccharides in Escherichia coli
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, Massachusetts 02115.
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