Cellobiose uptake in the hyperthermophilic archaeon Pyrococcus furiosus is mediated by an inducible, high-affinity ABC transporter

J Bacteriol. 2001 Sep;183(17):4979-84. doi: 10.1128/JB.183.17.4979-4984.2001.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / genetics
  • ATP-Binding Cassette Transporters / isolation & purification*
  • ATP-Binding Cassette Transporters / metabolism*
  • Cellobiose / metabolism*
  • Cloning, Molecular
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli
  • Kinetics
  • Molecular Weight
  • Pyrococcus / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • Cellobiose