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Applied and Environmental Microbiology, January 2001, p. 148-154, Vol. 67, No. 1
Environmental Research Division, Argonne
National Laboratory, Argonne, Illinois 60439,1
and Department of Microbiology, Southern Illinois University,
Carbondale, Illinois 629012
Received 16 August 2000/Accepted 19 October 2000
Escherichia coli NZN111 is blocked in the ability to
grow fermentatively on glucose but gave rise spontaneously to a mutant that had this ability. The mutant carries out a balanced fermentation of glucose to give approximately 1 mol of succinate, 0.5 mol of acetate, and 0.5 mol of ethanol per mol of glucose. The causative mutation was mapped to the ptsG gene, which encodes the
membrane-bound, glucose-specific permease of the phosphotransferase
system, protein EIICBglc. Replacement of the chromosomal
ptsG gene with an insertionally inactivated form also
restored growth on glucose and resulted in the same distribution of
fermentation products. The physiological characteristics of the
spontaneous and null mutants were consistent with loss of function of
the ptsG gene product; the mutants possessed greatly
reduced glucose phosphotransferase activity and lacked normal glucose
repression. Introduction of the null mutant into strains not blocked in
the ability to ferment glucose also increased succinate production in
those strains. This phenomenon was widespread, occurring in different
lineages of E. coli, including E. coli B.
0099-2240/01/$04.00+0 DOI: 10.1128/AEM.67.1.148-154.2001
Mutation of the ptsG Gene Results in
Increased Production of Succinate in Fermentation of Glucose by
Escherichia coli


*
Corresponding author. Mailing address: Argonne National
Laboratory, Bldg. 202/Rm. BE111, 9700 South Cass Avenue, Argonne, IL
60439. Phone: (630) 252-7432. Fax: (630) 252-7709. E-mail: donnelly{at}anl.gov.
Present address: Maxygen, Inc., Redwood City, CA 94063.
Present address: Genentech, Inc., South San Francisco, CA 94080.
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