Active Transport of Sugars into Escherichia coli

Henderson, Peter J. F.

doi:10.1007/978-1-4684-7679-8_11

Cited by 10 publications

(14 citation statements)

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“…Glucose is transported into the cell via two highaffinity active transport systems, which are synthesized maximally during growth under glucose limitation and require periplasmic glucose-binding proteins GBP1 and GBP2 (7). These GBP1-and GBP2-dependent systems, respectively, also transport galactose and xylose with high affinity, and their general properties indicate that they have much in common with the binding protein-dependent systems that transport sugars such as maltose, galactose, arabinose, and ribose into enteric bacteria (1,5,9,15). These latter systems have generally been shown to consist of a periplasmic binding protein, two transmembrane proteins, and at least one protein that is associated with the cytoplasmic surface of the membrane and binds ATP.…”

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confidence: 99%

“…These latter systems have generally been shown to consist of a periplasmic binding protein, two transmembrane proteins, and at least one protein that is associated with the cytoplasmic surface of the membrane and binds ATP. It is likely, although not proven, that the energy for transport is provided by the hydrolysis of ATP (1,5,15,16).Bacteria can also transport sugars by using proton-or cation-linked systems or via phosphoenolpyruvate-dependent phosphotransferase systems (5,15,23). Lactose transport has been extensively investigated in Escherichia coli and other enteric bacteria, in which it is catalyzed by a single transmembrane protein at the expense of the proton motive force generated by respiration or ATP hydrolysis (H+-lactose symport) (15,17,22).…”

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confidence: 99%

“…It is likely, although not proven, that the energy for transport is provided by the hydrolysis of ATP (1,5,15,16).…”

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confidence: 99%

“…Lactose transport has been extensively investigated in Escherichia coli and other enteric bacteria, in which it is catalyzed by a single transmembrane protein at the expense of the proton motive force generated by respiration or ATP hydrolysis (H+-lactose symport) (15,17,22). The transported lactose is subsequently hydrolyzed to galactose and glucose by Pgalactosidase.…”

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Binding-protein-dependent lactose transport in Agrobacterium radiobacter

1990

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, and isopropyl-,3-D-thiogalactoside and were subject to catabolite repression by glucose, galactose, and succinate which was not alleviated by cyclic AMP. We conclude that lactose is transported into A. radiobacter via a binding protein-dependent active transport system (in contrast to the H+ symport and phosphotransferase systems found in other bacteria) and that the expression of this transport system is closely linked to that of P-galactosidase.Agrobacterium radiobacter is a gram-negative aerobe that utilizes a wide range of sugars as sole carbon substrates for growth. Glucose is transported into the cell via two highaffinity active transport systems, which are synthesized maximally during growth under glucose limitation and require periplasmic glucose-binding proteins GBP1 and GBP2 (7). These GBP1-and GBP2-dependent systems, respectively, also transport galactose and xylose with high affinity, and their general properties indicate that they have much in common with the binding protein-dependent systems that transport sugars such as maltose, galactose, arabinose, and ribose into enteric bacteria (1,5,9,15). These latter systems have generally been shown to consist of a periplasmic binding protein, two transmembrane proteins, and at least one protein that is associated with the cytoplasmic surface of the membrane and binds ATP. It is likely, although not proven, that the energy for transport is provided by the hydrolysis of ATP (1,5,15,16).Bacteria can also transport sugars by using proton-or cation-linked systems or via phosphoenolpyruvate-dependent phosphotransferase systems (5,15,23). Lactose transport has been extensively investigated in Escherichia coli and other enteric bacteria, in which it is catalyzed by a single transmembrane protein at the expense of the proton motive force generated by respiration or ATP hydrolysis (H+-lactose symport) (15,17,22). The transported lactose is subsequently hydrolyzed to galactose and glucose by Pgalactosidase. The genes coding for the transport protein (lacl) and ,-galactosidase (lacZ) are part of the lac operon, which also codes for galactoside transacetylase (lacA) and the lac repressor (lad). Transcription is induced by lactose, melibiose, and isopropyl-p3-D-thiogalactoside (IPTG) (also * Corresponding author.

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confidence: 99%

mentioning

confidence: 99%

“…It is likely, although not proven, that the energy for transport is provided by the hydrolysis of ATP (1,5,15,16).…”

mentioning

confidence: 99%

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confidence: 99%

mentioning

confidence: 99%

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Binding-protein-dependent lactose transport in Agrobacterium radiobacter

1990

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The Molecular Biology of Sugar Transport Proteins

Henderson

Davis

McKeown

et al. 1991

Cell Membrane Transport

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Proton-linked sugar transport systems in bacteria

Henderson

1990

J Bioenerg Biomembr

156

108

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The cell membranes of various bacteria contain proton-linked transport systems for D-xylose, L-arabinose, D-galactose, D-glucose, L-rhamnose, L-fucose, lactose, and melibiose. The melibiose transporter of E. coli is linked to both Na+ and H+ translocation. The substrate and inhibitor specificities of the monosaccharide transporters are described. By locating, cloning, and sequencing the genes encoding the sugar/H+ transporters in E. coli, the primary sequences of the transport proteins have been deduced. Those for xylose/H+, arabinose/H+, and galactose/H+ transport are homologous to each other. Furthermore, they are just as similar to the primary sequences of the following: glucose transport proteins found in a Cyanobacterium, yeast, alga, rat, mouse, and man; proteins for transport of galactose, lactose, or maltose in species of yeast; and to a developmentally regulated protein of Leishmania for which a function is not yet established. Some of these proteins catalyze facilitated diffusion of the sugar without cation transport. From the alignments of the homologous amino acid sequences, predictions of common structural features can be made: there are likely to be twelve membrane-spanning alpha-helices, possibly in two groups of six; there is a central hydrophilic region, probably comprised largely of alpha-helix; the highly conserved amino acid residues (40-50 out of 472-522 total) form discrete patterns or motifs throughout the proteins that are presumably critical for substrate recognition and the molecular mechanism of transport. Some of these features are found also in other transport proteins for citrate, tetracycline, lactose, or melibiose, the primary sequences of which are not similar to each other or to the homologous series of transporters. The glucose/Na+ transporter of rabbit and man is different in primary sequence to all the other sugar transporters characterized, but it is homologous to the proline/Na+ transporter of E. coli, and there is evidence for its structural similarity to glucose/H+ transporters in Plants. In vivo and in vitro mutagenesis of the lactose/H+ and melibiose/Na+ (H+) transporters of E. coli has identified individual amino acid residues alterations of which affect sugar and/or cation recognition and parameters of transport. Most of the bacterial transport proteins have been identified and the lactose/H+ transporter has been purified. The directions of future investigations are discussed.

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Active Transport of Sugars into Escherichia coli

Cited by 10 publications

References 246 publications

Binding-protein-dependent lactose transport in Agrobacterium radiobacter

Binding-protein-dependent lactose transport in Agrobacterium radiobacter

The Molecular Biology of Sugar Transport Proteins

Proton-linked sugar transport systems in bacteria

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