Isolation and characterization of a mutation that alters the substrate specificity of the Escherichia coli glucose permease
Gail S. Begley, Kristy A. Warner, Jos C. Arents, P.W. Postma, Gary R. Jacobson
Abstract
Gail S. Begley, Kristy A. Warner, Jos C. Arents, P.W. Postma, Gary R. Jacobson
Abstract
We isolated 10 mannitol-positive mutants from a mannitol-negative Escherichia coli strain. These mutations mapped within ptsG, encoding the glucose permease (EIIGlc), and resulted in a G-320-to-V substitution that allows EIIGlc to transport mannitol. Gly-320 lies within a putative transmembrane helix of EIIGlc that may be involved in substrate recognition.
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We isolated 10 mannitol-positive mutants from a mannitol-negative Escherichia coli strain. These mutations mapped within ptsG, encoding the glucose permease (EIIGlc), and resulted in a G-320-to-V substitution that allows EIIGlc to transport mannitol. Gly-320 lies within a putative transmembrane helix of EIIGlc that may be involved in substrate recognition.
Key concepts: Permease, Escherichia coli, Biology, Mutant, Biochemistry, Mutation, Membrane transport protein, Mannitol