scholarly journals Characteristics of a Binding Protein-Dependent Transport System for sn-Glycerol-3-Phosphate in Escherichia coli That Is Part of the pho Regulon

1982 ◽  
Vol 150 (3) ◽  
pp. 1154-1163 ◽  
Author(s):  
Herbert Schweizer ◽  
Manfred Argast ◽  
Winfried Boos
Keyword(s):  
Escherichia Coli ◽  
Transport System ◽  
Binding Protein ◽  
Pho Regulon ◽  
Dependent Transport

scholarly journals Cellobiose Uptake in the Hyperthermophilic ArchaeonPyrococcus furiosus Is Mediated by an Inducible, High-Affinity ABC Transporter

2001 ◽  
Vol 183 (17) ◽  
pp. 4979-4984 ◽  
Author(s):  
Sonja M. Koning ◽  
Marieke G. L. Elferink ◽  
Wil N. Konings ◽  
Arnold J. M. Driessen
Keyword(s):  
Escherichia Coli ◽  
Gene Cluster ◽  
Abc Transporter ◽  
Transport System ◽  
Abc Transporters ◽  
Pyrococcus Furiosus ◽  
Binding Protein ◽  
Hyperthermophilic Archaeon ◽  
High Affinity ◽  
Dependent Transport

ABSTRACT The hyperthermophilic archaeon Pyrococcus furiosuscan utilize different β-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. furiosusmembranes to homogeneity as a 70-kDa glycoprotein. CbtA not only binds cellobiose but also cellotriose, cellotetraose, cellopentaose, laminaribiose, laminaritriose, and sophorose. The cbtAgene 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.

scholarly journals Periplasmic binding protein dependent transport system for maltose and maltodextrins: some recent studies

1989 ◽  
Vol 63 (1-2) ◽  
pp. 53-60
Author(s):  
W. Saurin ◽  
E. Francoz ◽  
P. Martineau ◽  
A. Charbit ◽  
E. Dassa ◽  
...  
Keyword(s):  
Transport System ◽  
Binding Protein ◽  
Periplasmic Binding Protein ◽  
Dependent Transport

Periplasmic binding protein-dependent transport systems: the membrane-associated components

1990 ◽  
Vol 326 (1236) ◽  
pp. 353-365 ◽  
Keyword(s):  
Transport System ◽  
Atp Hydrolysis ◽  
Binding Protein ◽  
Primary Source ◽  
Energy Coupling ◽  
Transport Systems ◽  
Common Mechanism ◽  
Atp Binding ◽  
Periplasmic Binding Protein ◽  
Dependent Transport

Periplasmic binding protein-dependent transport systems are multicomponent, consisting of several inner membrane-associated proteins and a periplasmic component. The membrane-associated components of different systems are related in organization and function suggesting that, despite different substrate specificities, each transport system functions by a common mechanism. Current understanding of these components is reviewed. The nature of energy coupling to periplasmic transport systems has long been debated. Recent data now demonstrate that ATP hydrolysis is the primary source of energy for transport. The ATP-binding transport components are the best characterized of a family of closely related ATP-binding proteins believed to couple ATP hydrolysis to a variety of different biological processes. Intriguingly, systems closely related to periplasmic binding protein-dependent transport systems have recently been identified in several Gram-positive organisms (which lack a periplasm) and in eukaryotic cells. This class of transport system appears to be widespread in nature, serving a variety of important and diverse functions.

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