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Article

A triple mutant, K319N/H322Q/E325Q, of the lactose permease cotransports H+ with thiodigalactoside.

The Journal of membrane biology - 1 Jun 2001

Johnson J L, Lockheart M S, Brooker R J

Abstract excerpt

In a previous study, we characterized a lactose permease mutant (K319N/E325Q) that can transport H+ ions with sugar. This result was surprising because other studies had suggested that Glu-325 plays an essential role in H+ binding. To determine if the lactose permease contains one or more auxiliary H+ binding sites, we began with the K319N/E325Q strain, which catalyzes a sugar-dependent H+ leak, and isolated...

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PMID: 11420608
DOI: 10.1007/s00232-001-0024-2

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TDG

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

A triple mutant, K319N/H322Q/E325Q, of the lactose permease cotransports H+ with thiodigalactoside.PMID 11420608Read ↗

An analysis of lactose permease "sugar specificity" mutations which also affect the coupling between proton and lactose transport. II. Second site revertants of the thiodigalactoside-dependent proton leak by the Val177/Asn319 permease.Semantic proximity Read ↗

A suppressor analysis of residues involved in cation transport in the lactose permease: identification of a coupling sensor.Semantic proximity Read ↗

Characterization of the double mutant, Val-177/Asn-322, of the lactose permease.Semantic proximity Read ↗

Evidence that the asparagine 322 mutant of the lactose permease transports protons and lactose with a normal stoichiometry and accumulates lactose against a concentration gradient.Semantic proximity Read ↗

Functional roles of Glu-269 and Glu-325 within the lactose permease of Escherichia coli.Semantic proximity Read ↗

An analysis of suppressor mutations suggests that the two halves of the lactose permease function in a symmetrical manner.Semantic proximity Read ↗

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Identification and characterization of functional residues in a Na+/H+ antiporter (NhaA) from Escherichia coli by random mutagenesis.Semantic proximity Read ↗

Characterization of Escherichia coli lactose carrier mutants that transport protons without a cosubstrate. Probes for the energy barrier to uncoupled transport.Semantic proximity Read ↗

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Suppressor analysis of mutations in the loop 2-3 motif of lactose permease: evidence that glycine-64 is an important residue for conformational changes.Semantic proximity Read ↗

Evidence for structural symmetry and functional asymmetry in the lactose permease of Escherichia coli.Semantic proximity Read ↗

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