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Journal of Bacteriology, April 1999, p. 2225-2235, Vol. 181, No. 7
Department of Microbiology, Molecular Biology
and Biochemistry, University of Idaho, Moscow, Idaho
83844-3052,1 and Department of Biology,
The John Muir College, University of California at San Diego, La
Jolla, California 92093-01162
Received 29 September 1998/Accepted 12 January 1999
The glucose analog 2-deoxyglucose (2dGlc) inhibits the growth and
multicellular development of Myxococcus xanthus. Mutants of
M. xanthus resistant to 2dGlc, designated hex
mutants, arise at a low spontaneous frequency. Expression of the
Escherichia coli glk (glucokinase) gene in M. xanthus
hex mutants restores 2dGlc sensitivity, suggesting that these
mutants arise upon the loss of a soluble hexokinase function that
phosphorylates 2dGlc to form the toxic intermediate,
2-deoxyglucose-6-phosphate. Enzyme assays of M. xanthus
extracts reveal a soluble hexokinase
(ATP:D-hexose-6-phosphotransferase; EC 2.7.1.1) activity
but no phosphotransferase system activities. The hex
mutants have lower levels of hexokinase activities than the wild type,
and the levels of hexokinase activity exhibited by the hex
mutants are inversely correlated with the ability of 2dGlc to inhibit
their growth and sporulation. Both 2dGlc and N-acetylglucosamine act as inhibitors of glucose turnover
by the M. xanthus hexokinase in vitro, consistent with the
finding that glucose and N-acetylglucosamine can antagonize
the toxic effects of 2dGlc in vivo.
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.
Mutations That Confer Resistance to 2-Deoxyglucose Reduce the
Specific Activity of Hexokinase from Myxococcus
xanthus
*
Corresponding author. Mailing address: Department of
Microbiology, Molecular Biology and Biochemistry, University of Idaho, Moscow, ID 83844-3052. Phone: (208) 885-0571. Fax: (208) 885-6518. E-mail: pay{at}uidaho.edu.
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