Lactose transport mutants of Escherichia coli resistant to inhibition by the phosphotransferase system.
The lactose carrier activity of Escherichia coli is inhibited by the binding of dephosphorylated glucose enzyme III. Saier et al. ((1978) J. Bacteriol. 133, 1358-1367) isolated lacY mutants that escaped this inhibition. This communication reports the cloning and sequencing of one of the Saier mutants and the isolation, cloning and sequencing of another similar mutant. Both mutations resulted in amino acid substitutions on the middle cytoplasmic loop of the carrier (alanine-198 to valine and serine-209 to isoleucine). It is concluded that this cytoplasmic loop may be one of the sites of binding of glucose enzyme III.
Wilson
T H
TH
Department of Cellular and Molecular Physiology, Harvard Medical School, Boston, MA 02115.
Yunker
P L
PL
Hansen
C L
CL
D001665:Binding Sites; D001692:Biological Transport; D002352:Carrier Proteins / Q000737:chemistry; D003001:Cloning, Molecular; D003593:Cytoplasm / Q000378:metabolism; D004352:Drug Resistance, Microbial; D004926:Escherichia coli / Q000187:drug effects / Q000235:genetics / Q000378:metabolism*; D007785:Lactose / Q000235:genetics / Q000378:metabolism*; D008757:Methylglucosides / Q000494:pharmacology; D008954:Models, Biological; D009154:Mutation; D010770:Phosphotransferases / Q000378:metabolism*
D002352:Carrier Proteins; D008757:Methylglucosides; D010770:Phosphotransferases; D007785:Lactose