The Maltose-Maltodextrin-Transport System of Escherichia coli K-12
Gram-negative bacteria inhabit a wide variety of environments and have evolved different strategies for capturing useful substances from the external milieu. Some active transport systems for sugars and amino acids are composed of a single polypeptide species. These systems usually function as secondary transporters that are energized by the electrochemical proton gradient. Examples of these are the permeases for ß-galactosides and glycerol-3-phosphate. In contrast to these “simple” systems, many growth substrates are transported by multicomponent systems that include a water-soluble substrate-binding protein in the periplasmic space, as well as proteins in the cytoplasmic membrane. These systems function as primary active transport systems that pump substrates into the cell at the expense of chemical energy. They are energized by an as yet undefined compound that is derived from the high-energy phosphoester pool of the cell (Berger, 1973; Berger and Heppel, 1974).
KeywordsOuter Membrane Cytoplasmic Membrane Periplasmic Space Hybrid Protein Active Transport System
Unable to display preview. Download preview PDF.
- Brass, J. M., Ehmann, U., and Bukau, B., 1984, Reconstitution of maltose transport in Escherichia coli Conditions affecting import of maltose binding protein into the periplasm of calcium treated cells, J. Bacteriol.,in press.507–514Google Scholar
- Dietzel, I., Kolb, V., and Boos, W., 1978, Pole cap formation in Escherichia coli following induction of the maltose binding protein, Arch. Mikrobiol. 118: 207–218.Google Scholar
- Luckey, M., and Nikaido, H., 1980, Specificity of diffusion channels produced by X-phage receptor protein of Escherichia coli, Proc. Natl. Acad. Sci. USA 77: 167–171.Google Scholar
- Neuhaus, J. M., 1982, The receptor protein of phage X: Purification, characterization and preliminary electrical studies in planar lipid bilayers, Ann. Microbiol. (Inst. Pasteur) 133A: 27–32.Google Scholar
- Parues, J. R., and Boos, W., 1973, Undirectional transport activity mediated by the galactose binding protein of Escherichia coli, J. Biol. Chem. 248: 4436–4445.Google Scholar
- Schwartz, M., 1967, Sur l’existence chez Escherichia coli K-12 d’une regulation commune a la biosynthése des recepteurs du bacteriophage lambda et au metabolisme du maltose, Ann. de !’Institut Pasteur 113: 685–704.Google Scholar
- Schwartz, M., 1980, Interaction of phages with their receptor proteins, in: Virus Receptors, Vol. 7 ( L. L. Randal and L. Philipson, eds.), Chapman and Hall, London, pp. 61–94.Google Scholar
- Szmelcman, S., Schwartz, M., Silhavy, M., and Boos, W., 1976, Maltose transport in Escherichia coli K-I2: A comparison of transport kinetics in wild-type and K-resistant mutants with the dissociation constants of the maltose binding protein as measured by fluorescence quenching, Eur. J. Biochem. 65: 13–19.PubMedCrossRefGoogle Scholar
- Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J., 1982, Distantly related sequences in the a and 13 subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold, Eur. Mol. Biol. Org. J. 1: 945–951.Google Scholar
- Wandersmann, C., Schwartz, M., and Ferenci, T., 1979, Mutants of Escherichia coli impaired in the transport of maltodextrins, J. Bacteriol. 140: 1–13.Google Scholar