scholarly journals Biochemical evidence for the presence of two α-glucoside ABC-transport systems in the hyperthermophilic archaeonPyrococcus furiosus

Archaea ◽  
2002 ◽  
Vol 1 (1) ◽  
pp. 19-25 ◽  
Author(s):  
Sonja M. Koning ◽  
Wil N. Konings ◽  
Arnold J.M. Driessen
Keyword(s):  
Transport System ◽  
Pyrococcus Furiosus ◽  
Binding Protein ◽  
Transport Systems ◽  
Atp Binding ◽  
Hyperthermophilic Archaeon ◽  
Biochemical Evidence ◽  
Abc Transport ◽  
Maltose Transporter ◽  
Atp Binding Cassette

The hyperthermophilic archaeonPyrococcus furiosuscan utilize different carbohydrates, such as starch, maltose and trehalose. Uptake of α-glucosides is mediated by two different, binding protein-dependent, ATP-binding cassette (ABC)-type transport systems. The maltose transporter also transports trehalose, whereas the maltodextrin transport system mediates the uptake of maltotriose and higher malto-oligosaccharides, but not maltose. Both transport systems are induced during growth on their respective substrates.

scholarly journals ATP-binding Cassette (ABC) Transport System Solute-binding Protein-guided Identification of Novel d-Altritol and Galactitol Catabolic Pathways inAgrobacterium tumefaciensC58

2015 ◽  
Vol 290 (48) ◽  
pp. 28963-28976 ◽  
Author(s):  
Daniel J. Wichelecki ◽  
Matthew W. Vetting ◽  
Liyushang Chou ◽  
Nawar Al-Obaidi ◽  
Jason T. Bouvier ◽  
...  
Keyword(s):  
Transport System ◽  
Binding Protein ◽  
Atp Binding ◽  
Catabolic Pathways ◽  
Abc Transport ◽  
Atp Binding Cassette

scholarly journals Archaeal Binding Protein-Dependent ABC Transporter: Molecular and Biochemical Analysis of the Trehalose/Maltose Transport System of the Hyperthermophilic Archaeon Thermococcus litoralis

1998 ◽  
Vol 180 (3) ◽  
pp. 680-689 ◽  
Author(s):  
Reinhold Horlacher ◽  
Karina B. Xavier ◽  
Helena Santos ◽  
Jocelyne DiRuggiero ◽  
Marina Kossmann ◽  
...  
Keyword(s):  
Transport System ◽  
Signal Sequence ◽  
Binding Protein ◽  
Inducible Promoter ◽  
Transport Systems ◽  
Thermococcus Litoralis ◽  
Hyperthermophilic Archaeon ◽  
E Coli ◽  
Transmembrane Segments ◽  
Maltose Transport

ABSTRACT We report the cloning and sequencing of a gene cluster encoding a maltose/trehalose transport system of the hyperthermophilic archaeonThermococcus litoralis that is homologous to themalEFG cluster encoding the Escherichia colimaltose transport system. The deduced amino acid sequence of themalE product, the trehalose/maltose-binding protein (TMBP), shows at its N terminus a signal sequence typical for bacterial secreted proteins containing a glyceride lipid modification at the N-terminal cysteine. The T. litoralis malE gene was expressed in E. coli under control of an inducible promoter with and without its natural signal sequence. In addition, in one construct the endogenous signal sequence was replaced by the E. coli MalE signal sequence. The secreted, soluble recombinant protein was analyzed for its binding activity towards trehalose and maltose. The protein bound both sugars at 85°C with aKd of 0.16 μM. Antibodies raised against the recombinant soluble TMBP recognized the detergent-soluble TMBP isolated from T. litoralis membranes as well as the products from all other DNA constructs expressed in E. coli. Transmembrane segments 1 and 2 as well as the N-terminal portion of the large periplasmic loop of the E. coli MalF protein are missing in the T. litoralis MalF. MalG is homologous throughout the entire sequence, including the six transmembrane segments. The conserved EAA loop is present in both proteins. The strong homology found between the components of this archaeal transport system and the bacterial systems is evidence for the evolutionary conservation of the binding protein-dependent ABC transport systems in these two phylogenetic branches.

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.

scholarly journals An Operon for a Putative ATP-Binding Cassette Transport System Involved in Acetoin Utilization ofBacillus subtilis

2000 ◽  
Vol 182 (19) ◽  
pp. 5454-5461 ◽  
Author(s):  
Ken-Ichi Yoshida ◽  
Yasutaro Fujita ◽  
S. Dusko Ehrlich
Keyword(s):  
Stationary Phase ◽  
Transport System ◽  
Minimal Medium ◽  
Atp Binding ◽  
Ofbacillus Subtilis ◽  
Abc Transport ◽  
Maximum Cell ◽  
Highly Hydrophobic ◽  
Single Operon ◽  
Atp Binding Cassette

ABSTRACT The ytrABCDEF operon of Bacillus subtiliswas deduced to encode a putative ATP-binding cassette (ABC) transport system. YtrB and YtrE could be the ABC subunits, and YtrC and YtrD are highly hydrophobic and could form a channel through the cell membrane, while YtrF could be a periplasmic lipoprotein for substrate binding. Expression of the operon was examined in cells grown in a minimal medium. The results indicate that the expression was induced only early in the stationary phase. The six ytr genes form a single operon, transcribed from a putative ςA-dependent promoter present upstream of ytrA. YtrA, which possesses a helix-turn-helix motif of the GntR family, acts probably as a repressor and regulates its own transcription. Inactivation of the operon led to a decrease in maximum cell yield and less-efficient sporulation, suggesting its involvement in the growth in stationary phase and sporulation. It is known that B. subtilis produces acetoin as an external carbon storage compound and then reuses it later during stationary phase and sporulation. When either the entireytr operon or its last gene, ytrF, was inactivated, the production of acetoin was not affected, but the reuse of acetoin became less efficient. We suggest that the Ytr transport system plays a role in acetoin utilization during stationary phase and sporulation.

scholarly journals Mechanistic Study of Utilization of Water-Insoluble Saccharomyces cerevisiae Glucans by Bifidobacterium breve Strain JCM1192

2017 ◽  
Vol 83 (7) ◽  
Author(s):  
Hoi Yee Keung ◽  
Tsz Kai Li ◽  
Lok To Sham ◽  
Man Kit Cheung ◽  
Peter Chi Keung Cheung ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Abc Transporter ◽  
Transport System ◽  
Binding Protein ◽  
Atp Binding ◽  
Carbohydrate Utilization ◽  
Content Type ◽  
Bifidobacterium Breve ◽  
Abc Transport ◽  
Atp Binding Protein

ABSTRACT Bifidobacteria exert beneficial effects on hosts and are extensively used as probiotics. However, due to the genetic inaccessibility of these bacteria, little is known about their mechanisms of carbohydrate utilization and regulation. Bifidobacterium breve strain JCM1192 can grow on water-insoluble yeast (Saccharomyces cerevisiae) cell wall glucans (YCWG), which were recently considered as potential prebiotics. According to the results of 1H nuclear magnetic resonance (NMR) spectrometry, the YCWG were composed of highly branched (1→3,1→6)-β-glucans and (1→4,1→6)-α-glucans. Although the YCWG were composed of 78.3% β-glucans and 21.7% α-glucans, only α-glucans were consumed by the B. breve strain. The ABC transporter (malEFG1) and pullulanase (aapA) genes were transcriptionally upregulated in the metabolism of insoluble yeast glucans, suggesting their potential involvement in the process. A nonsense mutation identified in the gene encoding an ABC transporter ATP-binding protein (MalK) led to growth failure of an ethyl methanesulfonate-generated mutant with yeast glucans. Coculture of the wild-type strain and the mutant showed that this protein was responsible for the import of yeast glucans or their breakdown products, rather than the export of α-glucan-catabolizing enzymes. Further characterization of the carbohydrate utilization of the mutant and three of its revertants indicated that this mutation was pleiotropic: the mutant could not grow with maltose, glycogen, dextrin, raffinose, cellobiose, melibiose, or turanose. We propose that insoluble yeast α-glucans are hydrolyzed by extracellular pullulanase into maltose and/or maltooligosaccharides, which are then transported into the cell by the ABC transport system composed of MalEFG1 and MalK. The mechanism elucidated here will facilitate the development of B. breve and water-insoluble yeast glucans as novel synbiotics. IMPORTANCE In general, Bifidobacterium strains are genetically intractable. Coupling classic forward genetics with next-generation sequencing, here we identified an ABC transporter ATP-binding protein (MalK) responsible for the import of insoluble yeast glucan breakdown products by B. breve JCM1192. We demonstrated the pleiotropic effects of the ABC transporter ATP-binding protein in maltose/maltooligosaccharide, raffinose, cellobiose, melibiose, and turanose transport. With the addition of transcriptional analysis, we propose that insoluble yeast glucans are broken down by extracellular pullulanase into maltose and/or maltooligosaccharides, which are then transported into the cell by the ABC transport system composed of MalEFG1 and MalK. The mechanism elucidated here will facilitate the development of B. breve and water-insoluble yeast glucans as novel synbiotics.

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 Full engagement of liganded maltose-binding protein stabilizes a semi-open ATP-binding cassette dimer in the maltose transporter

2015 ◽  
Vol 98 (5) ◽  
pp. 878-894 ◽  
Author(s):  
Frances Joan D. Alvarez ◽  
Cédric Orelle ◽  
Yan Huang ◽  
Ruchika Bajaj ◽  
R. Michael Everly ◽  
...  
Keyword(s):  
Binding Protein ◽  
Maltose Binding Protein ◽  
Atp Binding ◽  
Maltose Transporter ◽  
Atp Binding Cassette
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