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Journal of Bacteriology, November 2000, p. 6292-6301, Vol. 182, No. 22
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Maltose and Maltodextrin Transport in the Thermoacidophilic Gram-Positive Bacterium Alicyclobacillus acidocaldarius Is Mediated by a High-Affinity Transport System That Includes a Maltose Binding Protein Tolerant to Low pH

Anja Hülsmann,1 Rudi Lurz,2 Frank Scheffel,1 and Erwin Schneider1,*

Humboldt-Universität zu Berlin, Institut für Biologie/Bakterienphysiologie, D-10099 Berlin,1 and Max-Planck-Institut für Molekulare Genetik, D-14195 Berlin,2 Germany

Received 5 May 2000/Accepted 14 August 2000

We have studied the uptake of maltose in the thermoacidophilic gram-positive bacterium Alicyclobacillus acidocaldarius, which grows best at 57°C and pH 3.5. Under these conditions, accumulation of [14C]maltose was observed in cells grown with maltose but not in those grown with glucose. At lower temperatures or higher pH values, the transport rates substantially decreased. Uptake of radiolabeled maltose was inhibited by maltotetraose, acarbose, and cyclodextrins but not by lactose, sucrose, or trehalose. The kinetic parameters (Km of 0.91 ± 0.06 µM and Vmax ranging from 0.6 to 3.7 nmol/min/mg of protein) are consistent with a binding protein-dependent ATP binding cassette (ABC) transporter. A corresponding binding protein (MalE) that interacts with maltose with high affinity (Kd of 1.5 µM) was purified from the culture supernatant of maltose-grown cells. Immunoelectron microscopy revealed distribution of the protein throughout the cell wall. The malE gene was cloned and sequenced. Five additional open reading frames, encoding components of a maltose transport system (MalF and MalG), a putative transcriptional regulator (MalR), a cyclodextrinase (CdaA), and an alpha -glucosidase (GlcA), were identified downstream of malE. The malE gene lacking the DNA sequence that encodes the signal sequence was expressed in Escherichia coli. The purified wild-type and recombinant proteins bind maltose with high affinity over a wide pH range (2.5 to 7) and up to 80°C. Recombinant MalE cross-reacted with an antiserum raised against the wild-type protein, thereby indicating that the latter is the product of the malE gene. The MalE protein might be well suited as a model to study tolerance of proteins to low pH.

* Corresponding author. Mailing address: Humboldt-Universität zu Berlin, Institut für Biologie/Bakterienphysiologie, Chausseestr. 117, D-10115 Berlin, Germany. Phone: 49 (0)30-2093-8121. Fax: 49 (0)30-2093-8126. E-mail: erwin.schneider{at}rz.hu-berlin.de.

Journal of Bacteriology, November 2000, p. 6292-6301, Vol. 182, No. 22
0021-9193/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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