Phosphotransferase-System Enzymes as Chemoreceptors for Certain Sugars in Escherichia coli Chemotaxis

For D-glucose and analogs there are two distinct phosphotransferase enzymes II with different specificities. Transport and chemotaxis were studied in E. coli mutants having only one or the other of these two enzymes. It was found that the transport specificity of a given enzyme II correlates with ta...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 1974-07, Vol.71 (7), p.2895-2899
Main Authors: Adler, Julius, Epstein, Wolfgang
Format: Article
Language:English
Subjects:
Bacteria
Bacterial Proteins
Biological Sciences: Biochemistry
Biological Transport
Carrier Proteins
Chemoreceptor Cells
Chemoreceptors
Chemotaxis
Enzyme substrates
Enzymes
Escherichia coli - enzymology
Genotype
Glucose - metabolism
Glucosides
Mannose
Mutation
Phosphorylation
Phosphotransferases - metabolism
Receptors
Sugars
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Summary:For D-glucose and analogs there are two distinct phosphotransferase enzymes II with different specificities. Transport and chemotaxis were studied in E. coli mutants having only one or the other of these two enzymes. It was found that the transport specificity of a given enzyme II correlates with taxis specificity, and mutational loss of an enzyme II abolishes taxis toward only those sugars which it alone transports. Although enzyme I and the phosphate-carrier protein are required for full D-glucose taxis, it could not be determined if phosphorylation and transport are also required.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.71.7.2895