Bacterial solute uptake and efflux systems

Current Opinion in Microbiology

Volumn 1, Issue 2, 1998, Pages 248-253

  Lolkema, Juke S ^a   Poolman, Bert ^a   Konings, Wil N ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIA (MICROORGANISMS);

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; CARRIER PROTEIN;

CELL MEMBRANE POTENTIAL; CHEMISTRY; GRAM NEGATIVE BACTERIUM; GRAM POSITIVE BACTERIUM; METABOLISM; REVIEW; TRANSPORT AT THE CELLULAR LEVEL;

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEINS; BIOLOGICAL TRANSPORT; CARRIER PROTEINS; GRAM-NEGATIVE BACTERIA; GRAM-POSITIVE BACTERIA; MEMBRANE POTENTIALS;

EID: 0032034808     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1369-5274(98)80018-0     Document Type: Article

References (32)

1. Jacobs MHJ, van der Heide T, Driessen AJM, Konings WN: Glutamate transport in Rhodobacter sphaeroides is mediated by a novel binding protein-dependent secondary transport system. Proc Natl Acad Sci USA 1996, 93:12786-12790. Glutamate transport driven by ion motive force in membrane vesicles is strictly dependent on the presence of the glutamate binding protein. This is the first demonstration of an in vitro reconstitution of a binding-protein-dependent secondary transport system.
2. Driessen AJM, Jacobs MHJ, Konings WN: A new family of procaryotic transport proteins: binding protein dependent secondary transporters. Mol Microbiol 1997, 24:879-883. Databank search of putative binding protein-dependent secondary transporters. The results suggest that the membrane bound part of the transport system consists of a binding protein-independent secondary transporter and an additional membrane embedded part that is either present as part of the same polypeptide or as a separate subunit.
3. 4-dicarboxylate transport system, which is shown to be a member of a new class of binding protein-dependent secondary transporters.
4. Kaback HR: A molecular mechanism far energy coupling in a membrane transport protein, the lactose permease of Escherichia coli. Proc Natl Acad Sci USA 1997, 94:5539-5543. A model is proposed for the structural changes that occur in the protein upon binding of substrate and proton.
5. Lolkema JS, Poolman B: Uncoupling in secondary transport proteins. A mechanistic explanation for mutants of lac permease with an uncoupled phenotype. J Biol Chem 1995, 270:12670-12676.
6. Lolkema JS, Poolman B, Konings WN: Secondary transporters and metabolic energy generation in bacteria. In Handbook of Biological Physics. Edited by Konings WN, Kaback HR, Lolkema JS. Amsterdam: Elsevier Science; 1996:229-260.
7. Anantharam V, Allison MJ, Maloney PC: Oxalate: formate exchange. The basis for energy coupling in Oxalobacter formigenes. J Biol Chem 1989, 264:7244-7250.
8. Poolman B, Molenaar D, Smid EJ, Ubbink T, Abee T, Renault PP Konings WN: Malolactic fermentation: electrogenic uptake and malate/lactate antiport generate metabolic energy. J Bacteriol 1991, 173:6030-6037.
9. Abe K, Ruan Z-S, Maloney PC: Cloning, sequencing, and expression in Escherichia coli of OxIT, the oxalaterformate exchange protein of Oxalobacter formigenes. J Biol Chem 1996, 271:6789-6793. The primary structure is presented of OxIT which was one of the first secondary transporters that was shown to be involved in proton motive force generation. The amino acid sequence reveals that membrane potential generating secondary transporters are ordinary secondary transporters.
10. Bandell M, Ansanay V, Rachidi N, Dequin S, Lolkema JS: Membrane potential generating malate (MIeP) and citrate (CitP) transporters of lactic acid bacteria are homologous proteins. Substrate specificity of the 2-hydroxy-carboxylate transporter family. J Biol Chem 1997, 272:18140-18146. Analysis of the substrate specificity provide an rationale for the ability of the transporters to catalyze electrogenic precursor/product exchange which is the mode of transport under physiological conditions.
11. Higuchi T, Hayashi H, Abe K: Exchange of glutamate and γ aminobutyrate in a Lactocbacillus strain. J Bacteriol 1997, 179:3362-3364.
12. Abe K, Hayashi H, Maloney PC: Exchange of aspartate and alanine. Mechanism for the development of a proton-motive force in bacteria. J Biol Chem 1996, 271:3079-3084.
13. Salema M, Poolman B, Lolkema JS, Loureiro Dias MC, Konings WN: Uniport of monoanionic L-malate in membrane vesicles from Leuconostoc oenos. Eur J Biochem 1994, 225:289-295.
14. Ramos A, Poolman B, Santos H, Lolkema JS, Konings WN: Uniport of anionic citrate and proton consumption in citrate metabolism generates a proton motive force in Leuconostoc oenos. J Bacteriol 1994, 176:4899-4905.
15. Marty-Teysset C, Posthuma C, Lolkema JS, Schmitt P, Divies C, Konings WN: Proton motive force generation by citrolactic fermentation in Leuconostoc mesenteroides. J Bacteriol 1996, 178:2178-2185. Demonstration of secondary metabolic energy generation by citrate metabolism. Evidence is presented that the citrate transporter CitP catalyzes electrogenic citrate/laclate exchange under physiological conditions.
16. Marty-Teysset C, Lolkema JS, Schmitt P, Divies C, Konings WN: Membrane potential generating transport of citrate and malate catalysed by CitP of Leuconostoc mesenteroides. J Biol Chem 1995, 270:25370-25376.
17. Paulsen IT, Skurray RA, Tam R, Saier MH, Turner RJ, Weiner JH, Goldberg EB, Grínius LL: The SMR family: a novel family of multidrug efflux proteins involved with the efflux of lipophilic drugs. Mol Microbiol 1997 19:1167-1175.
18. Yerushalmi H, Lebendiker M, Schuldiner S: Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli. J Biol Chem 1996, 271:31044-31048.
19. Bolhuis H, Molenaar D, Van Veen HW, Poolman B, Driessen AJM, Konings WN: Multidrug resistance in Lactococcus lactis: evidence for ATP-dependent drug extrusion from the inner leaflet of the cytoplasmic membrane. EMBO J 1996, 15:4239-4245. Evidence is presented that multidrug resistance transporters pick up their substrates from the membrane rather than from the cytoplasm. The observations may contribute to the understanding of the apparent low specificity of the transporters for the substrates.
20. Bolhuis H, Van Veen HW, Brands JR, Putman M, Poolman B, Driessen AJW, Konings WN: Energetics and mechanisms of drug transport mediated by the lactococcal multidrug transporter LmrP. J Biol Chem 1996, 271:24123-24128.
21. Rosenberg MF Callaghan R, Ford RC, Higgins C F: Structure of the multidrug resistance P-glycoprotein to 2.5 nm resolution determined by electron microscopy and image analysis. J Biol Chem 1997, 272:10685-10694.
22. Quiocho FA, Ledvina PS: Atomic structure and specificity of bacterial periplasmic receptors for active transport and chemotaxis: variation of common themes. Mol Microbiol 1996, 20:17-25. Overview of the structural basis for ligand binding by the receptor components of binding-protein-dependent transport systems.
23. Dunten P, Mowbray SL: Crystal structure of the dipeptide binding protein from Escherichia coli involved in active transport and chemotaxis. Protein Sci 1995, 4:2327-2334.
24. Nickitenko AV, Trakhanov S, Quiocho FA: 2Å Resolution structure of DppA, a periplasmic dipeptide transport/chemosensory receptor. Biochemistry 1995, 34:16585-16595.
25. ds for the binding of dipeptides (low affinity) and tri/tetrapeptides (high affinity).
26. Tame JRH, Murshudow GN, Dodson EJ, Neil TK, Dodson GG, Higgins CF, Wilkinson AJ: The structural basis of sequence-independent peptide binding by OppA protein. Science 1994 264:1578-1581.
27. Ames GF-L, Liu CE, Joshi AK, Nikaido K: Liganded and unliganded receptors interact with equal affinity with the membrane complex of periplasmic permeases, a subfamily of traffic ATPases. J Biol Chem 1996, 271:14264-14270.
28. Liu CE, Liu P-Q, Ames GF-L: Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter). J Biol Chem 1997, 272:21883-21891.
29. Prossnitz E, Gee A, Ames GF: Reconstitution of the histidine periplasmic transport system in membrane vesicles. Energy coupling and interaction between the binding protein and the membrane complex. J Biol Chem 1989, 264:5006-5014.
30. Hall JA, Gehring JA, Nikaido H: Two modes of ligand binding in maltose binding protein of Escherichia coli: correlation with the structure of ligands and the structure of binding protein. J Biol Chem 1997, 272:17605-17609.
31. Hall JA, Thorgeirsson TE, Liu J, Shin Y-K, Nikaido H: Two modes of ligand binding in maltose binding protein of Escherichia coli: Electron paramagnetic resonance study of ligand-induced global conformational changes by site-directed spin labeling. J Biol Chem 1997, 272:17610-17614.
32. Hall JA, Ganesan AK, Chen J, Nikaido H: Two modes of ligand binding in maltose binding protein of Escherichia coli: functional significance in active transport J Biol Chem 1997, 272:17615-17622.