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Eukaryotic Cell, October 2002, p. 696-703, Vol. 1, No. 5
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.5.696-703.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Intracellular Maltose Is Sufficient To Induce MAL Gene Expression in Saccharomyces cerevisiae

Xin Wang, Mehtap Bali, Igor Medintz,{dagger} and Corinne A. Michels*

Queens College and Graduate School of City University of New York Biology Department, Flushing, New York 11367

Received 10 May 2002/ Accepted 26 June 2002

The presence of maltose induces MAL gene expression in Saccharomyces cells, but little is known about how maltose is sensed. Strains with all maltose permease genes deleted are unable to induce MAL gene expression. In this study, we examined the role of maltose permease in maltose sensing by substituting a heterologous transporter for the native maltose permease. PmSUC2 encodes a sucrose transporter from the dicot plant Plantago major that exhibits no significant sequence homology to maltose permease. When expressed in Saccharomyces cerevisiae, PmSUC2 is capable of transporting maltose, albeit at a reduced rate. We showed that introduction of PmSUC2 restores maltose-inducible MAL gene expression to a maltose permease-null mutant and that this induction requires the MAL activator. These data indicate that intracellular maltose is sufficient to induce MAL gene expression independently of the mechanism of maltose transport. By using strains expressing defective mal61 mutant alleles, we demonstrated a correlation between the rate of maltose transport and the level of the induction, which is particularly evident in medium containing very limiting concentrations of maltose. Moreover, our results indicate that a rather low concentration of intracellular maltose is needed to trigger MAL gene expression. We also showed that constitutive overexpression of either MAL61 maltose permease or PmSUC2 suppresses the noninducible phenotype of a defective mal13 MAL-activator allele, suggesting that this suppression is solely a function of maltose transport activity and is not specific to the sequence of the permease. Our studies indicate that maltose permease does not function as the maltose sensor in S. cerevisiae.


* Corresponding author. Mailing address: Queens College and Graduate School of CUNY Biology Department, 65-30 Kissena Blvd., Flushing, NY 11367. Phone: (718) 997-3400. Fax: (718) 997-3321. E-mail: Corinne_michels{at}qc.edu.

{dagger} Present address: Center for Bio/Molecular Science and Engineering, U.S. Naval Research Laboratory, Washington, DC 20375.


Eukaryotic Cell, October 2002, p. 696-703, Vol. 1, No. 5
1535-9778/02/$04.00+0     DOI: 10.1128/EC.1.5.696-703.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




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