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J Biol Chem, Vol. 274, Issue 20, 14006-14011, May 14, 1999
From the National Creative Research Initiative Center for
Behavioral Genetics, Department of Biological Sciences, Korea
Advanced Institute of Science and Technology, Yusong-Ku, Taejon,
Republic of Korea
Mutations arose from an Escherichia
coli strain defective in the high (Rbs/ribose) and low
(Als/allose and Xyl/xylose) affinity D-ribose transporters,
which allow cells to grow on D-ribose. Genetic tagging and
mapping of the mutations revealed that two loci in the E. coli linkage map are involved in creating a novel ribose
transport mechanism. One mutation was found in ptsG, the glucose-specific transporter of phosphoenolpyruvate:carbohydrate phosphotransferase system and the other in mlc, recently
reported to be involved in the regulation of ptsG. Five
different mutations in ptsG were characterized, whose
growth on D-ribose medium was about 80% that of the high
affinity system (Rbs+). Two of them were found in the
predicted periplasmic loops, whereas three others are in the
transmembrane region. Ribose uptakes in the mutants, competitively
inhibited by D-glucose, D-xylose, or
D-allose, were much lower than that of the high affinity
transporter but higher than those of the Als and Xyl systems. Further
analyses of the mutants revealed that the rbsK (ribokinase)
and rbsD (function unknown) genes are involved in the
ribose transport through PtsG, indicating that the phosphorylation of
ribose is not mediated by PtsG and that some unknown metabolic function
mediated by RbsD is required. It was also found that
D-xylose, another sugar not involved in phosphorylation,
was efficiently transported through the wild-type or mutant PtsG in
mlc-negative background. The efficiencies of xylose and
glucose transports are variable in the PtsG mutants, depending on their
locations, either in the periplasm or in the membrane. In an extreme
case of the transmembrane change (I283T), xylose transport is virtually
abolished, indicating that the residue is directly involved in
determining sugar specificity. We propose that there are at least two
domains for substrate specificity in PtsG with slightly altered
recognition properties.
A Mutated PtsG, the Glucose Transporter, Allows Uptake of
D-Ribose
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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