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Energization of the transport systems for arabinose and comparison with galactose transport in Escherichia coli

Research output: Contribution to journalArticle

K.R. Daruwalla, A.T. Paxton, P.J.F. Henderson

Original languageUndefined/Unknown
Pages (from-to)611-627
Number of pages17
JournalBiochemical Journal
Issue number3
Publication statusPublished - 1981

Bibliographical note

cited By (since 1996) 12

King's Authors


Strains of E. coli were obtained containing either the AraE or the AraF transport system for arabinose. AraE+, AraF- strains effected energized accumulation and displayed an arabinose-evoked alkaline pH change indicative of arabinose-H+ symport. In contrast, AraE-, AraF+ strains accumulated arabinose but did not display H+ symport. The ability of different sugars and their derivatives to elicit sugar-H+ symport in AraE+ strains was examined. Only L-arabinose and D-fucose were good substrates, and arabinose was the only inducer. Membrane vesicles prepared from an AraE+, AraF+ strain accumulated the sugar, energized most efficiently by the respiratory substrates ascorbate+phenazine methosulphate. Addition of arabinose or fucose to an anaerobic suspension of membrane vesicles caused an alkaline pH change indicative of sugar-H+ symport on the membrane-bound transport system. Kinetic studies and the effects of arsenate and uncoupling agents in intact cells and membrane vesicles gave further evidence that AraE is a low-affinity membrane-bound sugar-H+ symport system and that AraF is a binding-protein-dependent high-affinity system that does not require a transmembrane protonmotive force for energization. The interpretation of these results is that arabinose transport into E. coli is energized by an electrochemical gradient of protons (AraE system) or by phosphate bond energy (AraF system). In batch cultures the rates of growth and carbon cell yields on arabinose were lower in AraE-, AraF+ strains than in AraE+, AraF- or AraE+, AraF+ strains. The AraF system was more susceptible to catabolite repression than was the AraE system. The properties of the two transport systems for arabinose are compared with those of the genetically and biochemically distinct transport systems for galactose, GalP and MglP. It appears that AraE is analogous to GalP, and AraF to MglP.

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