Isolation and Sequencing of Escherichia coli Gene proP Reveals Unusual Structural Features of the Osmoregulatory Proline/Betaine transporter, ProP

Culham, Doreen E.; Lasby, Bonnie; Marangoni, Alejandro G.; Milner, Jocelyn L.; Steer, Brian A.; Nues, Rob W. van; Wood, Janet M.

doi:10.1006/jmbi.1993.1030

Cited by 158 publications

(182 citation statements)

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“…2B), was used for further analysis. We We also found that the final 213 nucleotides of our sequence showed 73% identity with the coding strand sequence downstream of the E. coli proP gene (11), not including a gap of 42 bases that are present in proP (and basRS; see above) but are not present in our sequence.…”

Section: Resultssupporting

confidence: 50%

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Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

et al. 1993

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Section: Resultssupporting

confidence: 50%

“…There was 13% cotransductional linkage between oxdB and pmrA (Table 2). These data ( The 50% lethal doses for strains LT2 (pmrA+), JKS1169 (TnlOdCam pmrA+), JKS5 (pmrA5O5), JKS1170 (TnlOd-Cam pmrA505), and JKS3 (pmrA503) were 11,8,20,000, 20,000, and 15,000 ng/ml, respectively. (B) Resistance to a CGE derived from human neutrophils.…”

Section: Resultsmentioning

confidence: 80%

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

et al. 1993

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“…GB transport in Escherichia coli is under osmotic control (27,29,30) and is mediated by two transport systems: the single component H ϩ -compatible solute cotransporter ProP (31) and the multicomponent transport system ProU (32,33). The ProU system is a member of the ATP-binding cassette superfamily (34,35) consisting of two cytoplasmic, membrane-associated ATPases, ProV; two integral membrane proteins, ProW; and a periplasmic ligand-binding protein, ProX (33).…”

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confidence: 99%

Cation-π Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli

Schiefner

Breed

Bösser

et al. 2004

Journal of Biological Chemistry

118

137

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Compatible solutes such as glycine betaine and proline betaine are accumulated to exceedingly high intracellular levels by many organisms in response to high osmolarity to offset the loss of cell water. They are excluded from the immediate hydration shell of proteins and thereby stabilize their native structure. Despite their exclusion from protein surfaces, the periplasmic ligand-binding protein ProX from the Escherichia coli ATP-binding cassette transport system ProU binds the compatible solutes glycine betaine and proline betaine with high affinity and specificity. To understand the mechanism of compatible solute binding, we determined the high resolution structure of ProX in complex with its ligands glycine betaine and proline betaine. This crystallographic study revealed that cation-interactions between the positive charge of the quaternary amine of the ligands and three tryptophan residues forming a rectangular aromatic box are the key determinants of the high affinity binding of compatible solutes by ProX. The structural analysis was combined with site-directed mutagenesis of the ligand binding pocket to estimate the contributions of the tryptophan residues involved in binding.

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“…These results were interpreted in terms of BetP comprising both functions of an osmosensor and an osmoregulator. This concept was first proposed for the Escherichia coli proline transporter ProP (8,9).…”

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Osmosensor and Osmoregulator Properties of the Betaine Carrier BetP from Corynebacterium glutamicum in Proteoliposomes

Rübenhagen¹,

Rönsch²,

Jung³

et al. 2000

Journal of Biological Chemistry

120

189

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The secondary glycine betaine uptake system BetP of Corynebacterium glutamicum was purified from Escherichia coli membranes in strep-tagged form after heterologous expression of the betP gene and was reconstituted in E. coli lipids. BetP retained its kinetic properties (V max and K m for betaine and Na ؉ ) as compared with intact cells. The influence of driving forces (Na ؉ gradient and/or electrical potential) on betaine uptake was quantified in proteoliposomes. BetP was effectively regulated by the external osmolality and was stimulated by the local anesthetic tetracaine. A shift of the optimum of osmotic stimulation to higher osmolalities was linearly correlated with an increasing share of phosphatidyl glycerol, the major lipid of the C. glutamicum plasma membrane in the E. coli lipid proteoliposomes. This finding correlates with results demonstrating an identical shift when betP was expressed in E. coli instead of C. glutamicum. These data indicate that (i) BetP comprises all elements of osmosensing and osmoregulatory mechanisms of betaine uptake, (ii) osmoregulation of BetP is directly related to protein/membrane interactions, (iii) the turgor pressure presumably plays no major role in osmoregulation of BetP, and (iv) the regulatory properties of BetP may be related to the physical state of the surrounding membrane.

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Isolation and Sequencing of Escherichia coli Gene proP Reveals Unusual Structural Features of the Osmoregulatory Proline/Betaine transporter, ProP

Cited by 158 publications

References 0 publications

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

Spontaneous pmrA mutants of Salmonella typhimurium LT2 define a new two-component regulatory system with a possible role in virulence

Cation-π Interactions as Determinants for Binding of the Compatible Solutes Glycine Betaine and Proline Betaine by the Periplasmic Ligand-binding Protein ProX from Escherichia coli

Osmosensor and Osmoregulator Properties of the Betaine Carrier BetP from Corynebacterium glutamicum in Proteoliposomes

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