Affiliation:
1. Department of Biology, University of Konstanz, D-7750 Konstanz, West Germany
Abstract
The starch polysaccharides amylose and amylopectin are not utilized by
Escherichia coli
, but are bound by the bacteria. The following evidence supports the view that the outer membrane λ receptor protein, a component of the maltose/ maltodextrin transport system is responsible for the binding. (i) Amylose and amylopectin both inhibit the transport of maltose into
E. coli
. (ii) Both polysaccharides prevent binding of non-utilizable maltodextrins by the intact bacterium, a process previously shown to be dependent on components of the maltose transport system (T. Ferenci, Eur. J. Biochem., in press). (iii) A fluorescent amylopectin derivative,
O
-(fluoresceinyl thiocarbamoyl)-amylopectin, has been synthesized and shown to bind to
E. coli
in a reversible, saturable manner. Binding of
O
-(fluoresceinyl thiocarbamoyl)-amylopectin is absent in mutants lacking the λ receptor, but mutations in any of the other components of the maltose transport system do not affect binding as long as λ receptor is present. (iv) Using the inhibition of λ receptor-dependent
O
-(fluoresceinyl thiocarbamoyl)-amylopectin binding as an assay, the affinities of the λ receptor for maltodextrins and other sugars have been estimated. The affinity for dextrins increases with increasing degree of polymerization (
K
d
for maltose, 14 mM; for maltotetraose, 0.3 mM; for maltodecaose, 0.075 mM). Maltose and some other di- and trisaccharides are inhibitory to amylopectin binding, but only at concentrations above 1 mM.
Publisher
American Society for Microbiology
Subject
Molecular Biology,Microbiology
Cited by
114 articles.
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