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Abstract

The maltose system consists of a number of genes that are under the control of a single transcriptional activator, the MalT protein. The proteins encoded are localized in different compartments of the cell, the cytoplasm, the periplasm, the cytoplasmic membrane and the outer membrane. This is probably the reason why the maltose system has become so attractive to scientists of different biological interests, and hence has become a model system for the analysis of many important biological functions:

  • The genetic approach used to elucidate the machinery of protein secretion employed the maltose system extensively and most sec genes have been defined using this system.1

  • The proteins comprising the complex transport system have become the standard for defining the function of binding protein-dependent ABC transporters in gram-negative bacteria.2–4

  • The modern methods of phoA- and lacZ-fusions used to elucidate the two-dimensional topology of membrane proteins were introduced using MalF, one of the intrinsic membrane proteins of the system.5

  • The λ-receptor, located in the outer membrane, was one of the first proteins recognized as a specific diffusion pore specifically catalyzing the entry of maltodextrins into the periplasm.6–9

  • The MalT-dependent regulation of the maltose genes was the first system recognized to be controlled by a purely positive acting and inducer-dependent transcriptional activator.10–12

  • The envelope localized λ-receptor has been used to genetically engineer surface located epitopes for the production of specific antibodies.13 Similarly, the periplasmic maltose-binding protein (MBP) has become a vehicle for export from E. coli of engineered proteins of eukaryotic origin.14–16

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Boos, W., Peist, R., Decker, K., Zdych, E. (1996). The Maltose System. In: Regulation of Gene Expression in Escherichia coli . Springer, Boston, MA. https://doi.org/10.1007/978-1-4684-8601-8_10

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