Cellobiose Uptake in the Hyperthermophilic Archaeon Pyrococcus furiosus Is Mediated by an Inducible, High-Affinity ABC Transporter
Sonja M. Koning, Marieke G. L. Elferink, Wil N. Konings, Arnold J. M. Driessen
Abstract
Sonja M. Koning, Marieke G. L. Elferink, Wil N. Konings, Arnold J. M. Driessen
Abstract
The hyperthermophilic archaeon Pyrococcus furiosus can utilize different beta-glucosides, like cellobiose and laminarin. Cellobiose uptake occurs with high affinity (K(m) = 175 nM) and involves an inducible binding protein-dependent transport system. The cellobiose binding protein (CbtA) was purified from P. furiosus membranes to homogeneity as a 70-kDa glycoprotein. CbtA not only binds cellobiose but also cellotriose, cellotetraose, cellopentaose, laminaribiose, laminaritriose, and sophorose. The cbtA gene was cloned and functionally expressed in Escherichia coli. cbtA belongs to a gene cluster that encodes a transporter that belongs to the Opp family of ABC transporters.
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The hyperthermophilic archaeon Pyrococcus furiosus can utilize different beta-glucosides, like cellobiose and laminarin. Cellobiose uptake occurs with high affinity (K(m) = 175 nM) and involves an inducible binding protein-dependent transport system. The cellobiose binding protein (CbtA) was purified from P. furiosus membranes to homogeneity as a 70-kDa glycoprotein. CbtA not only binds cellobiose but also cellotriose, cellotetraose, cellopentaose, laminaribiose, laminaritriose, and sophorose. The cbtA gene was cloned and functionally expressed in Escherichia coli. cbtA belongs to a gene cluster that encodes a transporter that belongs to the Opp family of ABC transporters.
Key concepts: Pyrococcus furiosus, Cellobiose, Biology, ATP-binding cassette transporter, Biochemistry, Escherichia coli, Transporter, Cellulosome