Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyrococcus furiosus英文文献资料.docVIP

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Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyrococcus furiosus英文文献资料.doc

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Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeon Pyrococcus furiosus英文文献资料

Archaea 1, 19–25 ? 2002 Heron Publishing—Victoria, Canada Biochemical evidence for the presence of two -glucoside ABC- transport systems in the hyperthermophilic archaeonPyrococcus furiosus SONJA M. KONING,1 WIL N. KONINGS1 and ARNOLD J. M. DRIESSEN1,2 1 Department of Microbiology, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, P. O. Box 14, 9750 AAHaren, The Netherlands 2 Author to whom correspondence should be addressed (a.j.m.driessen@biol.rug.nl) Received June 14, 2001; accepted September 14, 2001; published online October 11, 2001 Summary The hyperthermophilic archaeon Pyrococcus al. 1998, Greller et al. 1999). This system mediates the uptake of trehalose and maltose but not of maltodextrins. In contrast, a single maltose, trehalose and maltodextrin transporter has been described for the thermophilic bacterium Thermoanaero- bacter ethanolicus (Jones et al. 2000). The genome of P. furi- osus contains a gene cluster that encodes an ABC-type transporter that is nearly identical to the trehalose/maltose transporter of T. litoralis (DiRuggiero et al. 2000). In addition, it contains an operon that encodes a homolog of the maltose/ maltodextrin transporter of E. coli. Because the second trans- porter was found to be induced upon growth of P. furiosus on maltose, it was assumed that P. furiosus contains two maltose transport systems, one specific for maltose and trehalose and the other specific for maltose and maltodextrins (DiRuggiero et al. 2000). Here, we show that P. furiosus contains a tre- halose/maltose and a maltodextrin transport system. The latter system is specific for maltodextrins only and is not involved in maltose uptake. furiosus can utilize different carbohydrates, such as starch, maltose and trehalose. Uptake ofα-glucosides is mediated by two different, binding protein-dependent, ATP-binding cas- sette (ABC)-type transport systems. The maltose transporter also