The osmoprotectant proline betaine is a major substrate for the binding-protein-dependent transport system ProU of Escherichia coli K-12

1995 ◽  
Vol 246 (6) ◽  
pp. 783-796 ◽  
Author(s):  
Martin Haardt ◽  
Bettina Kempf ◽  
Elke Faatz ◽  
Erhard Bremer
2001 ◽  
Vol 183 (17) ◽  
pp. 4979-4984 ◽  
Author(s):  
Sonja M. Koning ◽  
Marieke G. L. Elferink ◽  
Wil N. Konings ◽  
Arnold J. M. Driessen

ABSTRACT The hyperthermophilic archaeon Pyrococcus furiosuscan utilize different β-glucosides, like cellobiose and laminarin. Cellobiose uptake occurs with high affinity (K m = 175 nM) and involves an inducible binding protein-dependent transport system. The cellobiose binding protein (CbtA) was purified from P. furiosusmembranes to homogeneity as a 70-kDa glycoprotein. CbtA not only binds cellobiose but also cellotriose, cellotetraose, cellopentaose, laminaribiose, laminaritriose, and sophorose. The cbtAgene was cloned and functionally expressed in Escherichia coli. cbtA belongs to a gene cluster that encodes a transporter that belongs to the Opp family of ABC transporters.


1998 ◽  
Vol 180 (18) ◽  
pp. 4828-4833 ◽  
Author(s):  
Roberto T. F. Celis ◽  
Peter F. Leadlay ◽  
Ipsita Roy ◽  
Anne Hansen

ABSTRACT In Escherichia coli K-12, the accumulation of arginine is mediated by two distinct periplasmic binding protein-dependent transport systems, one common to arginine and ornithine (AO system) and one for lysine, arginine, and ornithine (LAO system). Each of these systems includes a specific periplasmic binding protein, the AO-binding protein for the AO system and the LAO-binding protein for the LAO system. The two systems include a common inner membrane transport protein which is able to hydrolyze ATP and also phosphorylate the two periplasmic binding proteins. Previously, a mutant resistant to the toxic effects of canavanine, with low levels of transport activities and reduced levels of phosphorylation of the two periplasmic binding proteins, was isolated and characterized (R. T. F. Celis, J. Biol. Chem. 265:1787–1793, 1990). The gene encoding the transport ATPase enzyme (argK) has been cloned and sequenced. The gene possesses an open reading frame with the capacity to encode 268 amino acids (mass of 29.370 Da). The amino acid sequence of the protein includes two short sequence motifs which constitute a well-defined nucleotide-binding fold (Walker sequences A and B) present in the ATP-binding subunits of many transporters. We report here the isolation of canavanine-sensitive derivatives of the previously characterized mutant. We describe the properties of these suppressor mutations in which the transport of arginine, ornithine, and lysine has been restored. In these mutants, the phosphorylation of the AO- and LAO-binding proteins remains at a low level. This information indicates that whereas hydrolysis of ATP by the transport ATPase is an obligatory requirement for the accumulation of these amino acids in E. coli K-12, the phosphorylation of the periplasmic binding protein is not related to the function of the transport system.


1989 ◽  
Vol 63 (1-2) ◽  
pp. 53-60
Author(s):  
W. Saurin ◽  
E. Francoz ◽  
P. Martineau ◽  
A. Charbit ◽  
E. Dassa ◽  
...  

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