The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

malE  -  maltose transporter subunit

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK4026, JW3994, malJ
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of malE


High impact information on malE

  • Deletion of these REP sequences from the chromosomal operon not only destabilizes upstream malE mRNA, but also results in a 9-fold reduction in the synthesis of MalE protein [6].
  • Intragenic suppressor mutations of malE delta 12-18 have been obtained, some highly efficient in their ability to restore proper MBP export [7].
  • A deletion mutation, malE delta 12-18, removes seven residues from the hydrophobic core of the maltose binding protein (MBP) signal peptide and thus prevents secretion of this protein to the periplasm of E. coli [7].
  • Using a malE signal sequence mutant, which has a Mal-phenotype in secG mutant strains, we have isolated extragenic Mal+ suppressors [8].
  • Mutations in any of the three high-affinity binding sites reduced both malEp and malKp activity [9].

Biological context of malE


Anatomical context of malE


Associations of malE with chemical compounds

  • The sequences of the malE gene and of its mature product, the maltose-binding protein, have been determined and are in good agreement [15].
  • The malE gene encodes the pre-protein (396 amino acid residues) which yields, upon cleavage of the NH2-terminal extension (26 amino acid residues), the mature maltose-binding protein (370 amino acid residues) [15].
  • The induction of a specific abnormal malE-lacZ fusion protein, which is capable of disrupting the normal membrane protein secretion process, also increased the rate of killing by streptomycin [16].
  • In the other study, dominant mutations in malE (the structural gene of MBP) were isolated; one of these altered the same tyrosine residue (210) to cysteine [17].
  • These plasmids could be grouped into three classes, based upon their ability to complement in vivo a chromosomal malE deletion in the presence or absence of isopropyl thiogalactoside [18].

Physical interactions of malE

  • Another fusion gene was generated by inserting ceaB3 between the malE gene encoding maltose binding protein (mbp) and lacZ alpha of the pmal-c2 vector [19].

Regulatory relationships of malE

  • The in vivo synthesis and export of plasmid-encoded MBP were studied in the presence and absence of isopropyl thiogalactoside and maltose and in a strain harboring a prlA mutation that suppresses the malE signal sequence mutation and is thought to alter the export machinery of cells [18].
  • Mutations previously designated prlD were described that suppressed malE signal sequence mutations and were located in the vicinity of the secA gene on the Escherichia coli chromosome [20].

Other interactions of malE

  • To facilitate purification and characterization of SoxS, we constructed a fusion of soxS to malE, which encodes maltose-binding protein, and demonstrated that the in vivo expression of the MalE-SoxS fusion protein can provide SoxS function to a soxRS deletion mutant [21].
  • Moreover, when expressed in attenuated aroA S. typhimurium strain SL3261, the plasmids carrying malE and malE-HIV genes were stable in vitro and in vivo [22].

Analytical, diagnostic and therapeutic context of malE

  • To assess the molecular determinants of Kr resistance, the S. cinnamoneus tuf gene was expressed in Escherichia coli as a translational fusion to malE, which enabled the recovery by affinity chromatography of the recombinant protein uncontaminated by the host factor [23].


  1. Mechanism of maltose transport in Escherichia coli: transmembrane signaling by periplasmic binding proteins. Davidson, A.L., Shuman, H.A., Nikaido, H. Proc. Natl. Acad. Sci. U.S.A. (1992) [Pubmed]
  2. Comparison of sequences from the malB regions of Salmonella typhimurium and Enterobacter aerogenes with Escherichia coli K12: a potential new regulatory site in the interoperonic region. Dahl, M.K., Francoz, E., Saurin, W., Boos, W., Manson, M.D., Hofnung, M. Mol. Gen. Genet. (1989) [Pubmed]
  3. A mutation in the receiver domain of the Agrobacterium tumefaciens transcriptional regulator VirG increases its affinity for operator DNA. Han, D.C., Winans, S.C. Mol. Microbiol. (1994) [Pubmed]
  4. Purification and characterization of EpiD, a flavoprotein involved in the biosynthesis of the lantibiotic epidermin. Kupke, T., Stevanović, S., Sahl, H.G., Götz, F. J. Bacteriol. (1992) [Pubmed]
  5. A mutant form of maltose-binding protein of Escherichia coli deficient in its interaction with the bacteriophage lambda receptor protein. Bavoil, P., Wandersman, C., Schwartz, M., Nikaido, H. J. Bacteriol. (1983) [Pubmed]
  6. Differential mRNA stability controls relative gene expression within a polycistronic operon. Newbury, S.F., Smith, N.H., Higgins, C.F. Cell (1987) [Pubmed]
  7. Intragenic suppressor mutations that restore export of maltose binding protein with a truncated signal peptide. Bankaitis, V.A., Rasmussen, B.A., Bassford, P.J. Cell (1984) [Pubmed]
  8. A new genetic selection identifies essential residues in SecG, a component of the Escherichia coli protein export machinery. Bost, S., Belin, D. EMBO J. (1995) [Pubmed]
  9. Three adjacent binding sites for cAMP receptor protein are involved in the activation of the divergent malEp-malKp promoters. Vidal-Ingigliardi, D., Raibaud, O. Proc. Natl. Acad. Sci. U.S.A. (1991) [Pubmed]
  10. The nucleotide sequence of the gene for malF protein, an inner membrane component of the maltose transport system of Escherichia coli. Repeated DNA sequences are found in the malE-malF intercistronic region. Froshauer, S., Beckwith, J. J. Biol. Chem. (1984) [Pubmed]
  11. RcsC-mediated induction of colanic acid by secretion of streptokinase in Escherichia coli K-12. Lee, S.H., Kim, I.C., Lee, W.S., Byun, S.M. FEMS Microbiol. Lett. (1996) [Pubmed]
  12. Silent and functional changes in the periplasmic maltose-binding protein of Escherichia coli K12. I. Transport of maltose. Duplay, P., Szmelcman, S., Bedouelle, H., Hofnung, M. J. Mol. Biol. (1987) [Pubmed]
  13. Translocation of colicin E1 through cytoplasmic membrane of Escherichia coli. Yamada, M., Miki, T., Nakazawa, A. FEBS Lett. (1982) [Pubmed]
  14. Mutations in tar suppress defects in maltose chemotaxis caused by specific malE mutations. Manson, M.D., Kossmann, M. J. Bacteriol. (1986) [Pubmed]
  15. Sequences of the malE gene and of its product, the maltose-binding protein of Escherichia coli K12. Duplay, P., Bedouelle, H., Fowler, A., Zabin, I., Saurin, W., Hofnung, M. J. Biol. Chem. (1984) [Pubmed]
  16. Effects of production of abnormal proteins on the rate of killing of Escherichia coli by streptomycin. Wyka, M.A., St John, A.C. Antimicrob. Agents Chemother. (1990) [Pubmed]
  17. Genetic analysis of periplasmic binding protein dependent transport in Escherichia coli. Each lobe of maltose-binding protein interacts with a different subunit of the MalFGK2 membrane transport complex. Hor, L.I., Shuman, H.A. J. Mol. Biol. (1993) [Pubmed]
  18. In vivo and in vitro synthesis of Escherichia coli maltose-binding protein under regulatory control of the lacUV5 promoter-operator. Rasmussen, B.A., MacGregor, C.H., Ray, P.H., Bassford, P.J. J. Bacteriol. (1985) [Pubmed]
  19. A monoclonal antibody generated against a recombinant peptide fragment of the B3 domain of carcinoembryonic antigen reacts with intact carcinoembryonic antigen. Hagendorff, G., Hanes, J., von der Kammer, H., Scheit, K.H. Biochim. Biophys. Acta (1995) [Pubmed]
  20. Novel secA alleles improve export of maltose-binding protein synthesized with a defective signal peptide. Fikes, J.D., Bassford, P.J. J. Bacteriol. (1989) [Pubmed]
  21. Purification of a MalE-SoxS fusion protein and identification of the control sites of Escherichia coli superoxide-inducible genes. Fawcett, W.P., Wolf, R.E. Mol. Microbiol. (1994) [Pubmed]
  22. Studies of the anaerobically induced promoter pnirB and the improved expression of bacterial antigens. Newton, S.M., Klebba, P.E., Hofnung, M., Charbit, A. Res. Microbiol. (1995) [Pubmed]
  23. Natural kirromycin resistance of elongation factor Tu from the kirrothricin producer Streptomyces cinnamoneus. Cappellano, C., Monti, F., Sosio, M., Donadio, S., Sarubbi, E. Microbiology (Reading, Engl.) (1997) [Pubmed]
WikiGenes - Universities