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Gene Review

MAL11  -  Mal11p

Saccharomyces cerevisiae S288c

Synonyms: AGT1, General alpha-glucoside permease, MAL1T, MTP1, Maltose permease MAL11, ...
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High impact information on MAL11

  • Analysis of the MTP1 gene and its translation product mtTBP may provide an insight into the evolutionary origin of linear mitochondrial genomes and the role it plays in their replication and maintenance [1].
  • AGT1 expression is maltose inducible and induction is mediated by the Mal-activator [2].
  • Like Mal61p, Agt1p is a high-affinity, maltose/proton symporter, but Mal61p is capable of transporting only maltose and turanose, while Agt1p transports these two alpha-glucosides as well as several others including isomaltose, alpha-methylglucoside, maltotriose, palatinose, trehalose and melezitose [2].
  • Molecular genetic analysis is used to characterize the AGT1 gene encoding an alpha-glucoside transporter [2].
  • The sequence of the upstream region of AGT1 is identical to that of the maltose-inducible MAL61 gene over a 469 bp region containing the UASMAL but the 315 bp sequence immediately upstream of AGT1 shows no significant homology to the sequence immediately upstream of MAL61 [2].

Biological context of MAL11


Anatomical context of MAL11

  • Our results show that pNPalphaG is actively transported by S. cerevisiae cells by a H+-symport mechanism, which depends on the electrochemical proton gradient across the plasma membrane. pNPalphaG uptake is mediated by the AGT1 alpha-glucoside permease, which has a high affinity (Km=3 mM) for this chromogenic substrate [8].

Associations of MAL11 with chemical compounds

  • In contrast, expression of the maltose permease gene (MAL11) and maltose utilization is normal [9].
  • Our results indicate that the maltose-H+ symporters encoded by MAL11, MAL21, and MAL41 are not responsible for the trehalose transport activity [10].
  • In a yeast strain deleted for HXT1-17, GAL2, AGT1, YDL247w and YJR160c, glucose consumption and transport activity were completely abolished [11].
  • Maltotriose utilization from the permease encoded by AGT1 was regulated by the same genetic mechanisms as those involving the maltose transcriptional activator [7].
  • We show here that MAL64c has in addition pleiotropic effects on sugar fermentation: MAL64c strains constitutively synthesize an alpha-methylglucosidase and can complement a new gene, MTP1, for the fermentation of melezitose and alpha-methylglucoside [12].

Other interactions of MAL11

  • However, expression of Mty1p restores growth of the S. cerevisiae receptor strain on both maltose and maltotriose, whereas the closely related Mal31p supports growth on maltose only and Agt1p supports growth on a wider range of substrates, including maltose and maltotriose [13].
  • Known pleiotropic genes PDR5 and MAL11 are more accurately represented by the model than by a clustering procedure that requires genes to belong to a single cluster [14].
  • Evidence is presented that these two classes of mutants identify both a gene involved in the regulation of maltose identify both a gene involved in the regulation of maltose fermentation (MAL1R) and a gene involved in maltose transport (MAL1T) [15].


  1. Mitochondrial telomere-binding protein from Candida parapsilosis suggests an evolutionary adaptation of a nonspecific single-stranded DNA-binding protein. Nosek, J., Tomáska, L., Pagácová, B., Fukuhara, H. J. Biol. Chem. (1999) [Pubmed]
  2. Characterization of AGT1 encoding a general alpha-glucoside transporter from Saccharomyces. Han, E.K., Cotty, F., Sottas, C., Jiang, H., Michels, C.A. Mol. Microbiol. (1995) [Pubmed]
  3. Characterization of Saccharomyces cerevisiae strains from spontaneously fermented maize dough by profiles of assimilation, chromosome polymorphism, PCR and MAL genotyping. Hayford, A.E., Jespersen, L. J. Appl. Microbiol. (1999) [Pubmed]
  4. Multiple alpha-glucoside transporter genes in brewer's yeast. Jespersen, L., Cesar, L.B., Meaden, P.G., Jakobsen, M. Appl. Environ. Microbiol. (1999) [Pubmed]
  5. Two distinct pathways for trehalose assimilation in the yeast Saccharomyces cerevisiae. Jules, M., Guillou, V., François, J., Parrou, J.L. Appl. Environ. Microbiol. (2004) [Pubmed]
  6. Characterization and functional analysis of the MAL and MPH Loci for maltose utilization in some ale and lager yeast strains. Vidgren, V., Ruohonen, L., Londesborough, J. Appl. Environ. Microbiol. (2005) [Pubmed]
  7. Molecular analysis of maltotriose transport and utilization by Saccharomyces cerevisiae. Day, R.E., Rogers, P.J., Dawes, I.W., Higgins, V.J. Appl. Environ. Microbiol. (2002) [Pubmed]
  8. Colorimetric determination of active alpha-glucoside transport in Saccharomyces cerevisiae. Hollatz, C., Stambuk, B.U. J. Microbiol. Methods (2001) [Pubmed]
  9. Glucose uptake and metabolism in grr1/cat80 mutants of Saccharomyces cerevisiae. Ozcan, S., Schulte, F., Freidel, K., Weber, A., Ciriacy, M. Eur. J. Biochem. (1994) [Pubmed]
  10. Expression of high-affinity trehalose-H+ symport in Saccharomyces cerevisiae. Stambuk, B.U., Panek, A.D., Crowe, J.H., Crowe, L.M., de Araujo, P.S. Biochim. Biophys. Acta (1998) [Pubmed]
  11. Concurrent knock-out of at least 20 transporter genes is required to block uptake of hexoses in Saccharomyces cerevisiae. Wieczorke, R., Krampe, S., Weierstall, T., Freidel, K., Hollenberg, C.P., Boles, E. FEBS Lett. (1999) [Pubmed]
  12. MAL64c is a global regulator of alpha-glucoside fermentation: identification of a new gene involved in melezitose fermentation. Perkins, E.L., Needleman, R.B. Curr. Genet. (1988) [Pubmed]
  13. Maltotriose utilization by industrial Saccharomyces strains: characterization of a new member of the alpha-glucoside transporter family. Salema-Oom, M., Valadão Pinto, V., Gonçalves, P., Spencer-Martins, I. Appl. Environ. Microbiol. (2005) [Pubmed]
  14. A latent variable model for chemogenomic profiling. Flaherty, P., Giaever, G., Kumm, J., Jordan, M.I., Arkin, A.P. Bioinformatics (2005) [Pubmed]
  15. Mutational analysis of the MAL1 locus of Saccharomyces: identification and functional characterization of three genes. Cohen, J.D., Goldenthal, M.J., Buchferer, B., Marmur, J. Mol. Gen. Genet. (1984) [Pubmed]
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