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

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.

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Characterization of bacteriocin ABC transporter ATP-binding protein produced by a newly isolated Enterococcus casseliflavus MI001 strain

Beni-Suef University Journal of Basic and Applied Sciences ◽

10.1186/s43088-019-0006-z ◽

2019 ◽

Vol 8 (1) ◽

Cited By ~ 1

Author(s):

Indira Mikkili ◽

Venkateswarulu TC ◽

Abraham Peele Karlapudi ◽

Vidya Prabhakar Kodali ◽

Krupanidhi Srirama

Keyword(s):

Abc Transporter ◽

Specific Activity ◽

Binding Protein ◽

Gel Filtration ◽

Exchange Chromatography ◽

Food Preservation ◽

Atp Binding ◽

Transporter Protein ◽

Enterococcus Casseliflavus ◽

Atp Binding Protein

Abstract Background ATP-binding cassette (ABC) transporters constitute one of the largest transporter protein families and play a role in diverse biological processes. Results In the present study, bacteriocin isolated from the Enterococcus casseliflavus MI001 strain was identified as an ABC transporter ATP-binding protein. The optimal conditions for the production of bacteriocin were found to be at 35 °C, a pH 5.5, and an incubation time of 24 h. Purification was performed using ammonium sulphate precipitation, gel filtration, and DEAE ion exchange chromatography. The bacteriocin was purified with an eightfold purification scheme resulting with a specific activity of 15,000 AU/mg. The NMR spectrum of purified bacteriocin revealed the presence of amino acids, namely lysine, methionine, cysteine, proline, threonine, tryptophan, and histidine. Further, the bacteriocin ABC transporter showed antimicrobial activity against food spoilage microorganisms. Conclusions The ABC transporter ATP-binding protein could be used as a potential alternative for food preservation, and it may be considered as a bio-preservative agent in food processing industries.

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Oxidative stress induces phosphorylation of the ABC transporter, ATP-binding protein, in Porphyromonas gingivalis

Journal of Oral Science ◽

10.2334/josnusd.52.561 ◽

2010 ◽

Vol 52 (4) ◽

pp. 561-566 ◽

Cited By ~ 3

Author(s):

Takao Toyoda ◽

Soichiro Okano ◽

Yasuko Shibata ◽

Yoshimitsu Abiko

Keyword(s):

Oxidative Stress ◽

Porphyromonas Gingivalis ◽

Abc Transporter ◽

Binding Protein ◽

Atp Binding ◽

Atp Binding Protein

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

Journal of Biological Chemistry ◽

10.1074/jbc.m115.686857 ◽

2015 ◽

Vol 290 (48) ◽

pp. 28963-28976 ◽

Cited By ~ 20

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

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

Archaea ◽

10.1155/2002/529610 ◽

2002 ◽

Vol 1 (1) ◽

pp. 19-25 ◽

Cited By ~ 31

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.

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Erratum to: An ABC transporter complex containing S-adenosylmethionine (SAM)-induced ATP-binding protein is involved in antibiotics production and SAM signaling in Streptomyces coelicolor M145

Biotechnology Letters ◽

10.1007/s10529-012-1070-9 ◽

2012 ◽

Vol 35 (6) ◽

pp. 985-985

Author(s):

Sung-Kwon Lee ◽

SangJoon Mo ◽

Joo-Won Suh

Keyword(s):

Abc Transporter ◽

Binding Protein ◽

Streptomyces Coelicolor ◽

Atp Binding ◽

Atp Binding Protein

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An ABC transporter complex containing S-adenosylmethionine (SAM)-induced ATP-binding protein is involved in antibiotics production and SAM signaling in Streptomyces coelicolor M145

Biotechnology Letters ◽

10.1007/s10529-012-0987-3 ◽

2012 ◽

Vol 34 (10) ◽

pp. 1907-1914 ◽

Cited By ~ 5

Author(s):

Sung-Kwon Lee ◽

SangJoon Mo ◽

Joo-Won Suh

Keyword(s):

Abc Transporter ◽

Binding Protein ◽

Streptomyces Coelicolor ◽

Atp Binding ◽

Atp Binding Protein

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The Adhesion-Associated sca Operon inStreptococcus gordonii Encodes an Inducible High-Affinity ABC Transporter for Mn2+ Uptake

Journal of Bacteriology ◽

10.1128/jb.180.2.290-295.1998 ◽

1998 ◽

Vol 180 (2) ◽

pp. 290-295 ◽

Cited By ~ 88

Author(s):

Paul E. Kolenbrander ◽

Roxanna N. Andersen ◽

Rachel A. Baker ◽

Howard F. Jenkinson

Keyword(s):

Abc Transporter ◽

Binding Protein ◽

Transformation Process ◽

Atp Binding ◽

Wild Type ◽

High Affinity ◽

Transformation Medium ◽

Low Concentrations ◽

Atp Binding Protein ◽

Mutant Cells

ABSTRACT ScaA lipoprotein in Streptococcus gordonii is a member of the LraI family of homologous polypeptides found among streptococci, pneumococci, and enterococci. It is the product of the third gene within the scaCBA operon encoding the components of an ATP-binding cassette (ABC) transporter system. Inactivation ofscaC (ATP-binding protein) or scaA(substrate-binding protein) genes resulted in both impaired growth of cells and >70% inhibition of 54Mn2+ uptake in media containing <0.5 μM Mn2+. In wild-type andscaC mutant cells, production of ScaA was induced at low concentrations of extracellular Mn2+ (<0.5 μM) and by the addition of ≥20 μM Zn2+. Sca permease-mediated uptake of 54Mn2+ was inhibited by Zn2+ but not by Ca2+, Mg2+, Fe2+, or Cu2+. Reduced uptake of54Mn2+ by sca mutants and by wild-type cells in the presence of Zn2+ was abrogated by the uncoupler carbonylcyanide m-chlorophenylhydrazone, suggesting that Mn2+ uptake under these conditions was proton motive force dependent. The frequency of DNA-mediated transformation was reduced >20-fold in sca mutants. The addition of 0.1 mM Mn2+ to the transformation medium restored only partly the transformability of mutant cells, implying an alternate role for Sca proteins in the transformation process. Cells ofsca mutants were unaffected in other binding properties tested and were unaffected in sensitivity to oxidants. The results show that Sca permease is a high-affinity mechanism for the acquisition of Mn2+ and is essential for growth of streptococci under Mn2+-limiting conditions.

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Cloning and Sequencing of ABC Transporter ATP-Binding Protein Encoding Gene from Streptomyces minoensis

Biotechnology(Faisalabad) ◽

10.3923/biotech.2008.182.187 ◽

2008 ◽

Vol 7 (2) ◽

pp. 182-187

Author(s):

Laleh Zereshki N ◽

Reza Azarbaijan ◽

Mostafa Valizadeh ◽

Mohammad Saeid Heja

Keyword(s):

Abc Transporter ◽

Binding Protein ◽

Atp Binding ◽

Cloning And Sequencing ◽

Protein Encoding ◽

Encoding Gene ◽

Atp Binding Protein

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Characterization of the Binding Protein-Dependent Cellobiose and Cellotriose Transport System of the Cellulose Degrader Streptomyces reticuli

Applied and Environmental Microbiology ◽

10.1128/aem.65.6.2636-2643.1999 ◽

1999 ◽

Vol 65 (6) ◽

pp. 2636-2643 ◽

Cited By ~ 53

Author(s):

Andreas Schlösser ◽

Jens Jantos ◽

Karl Hackmann ◽

Hildgund Schrempf

Keyword(s):

Abc Transporter ◽

Binding Protein ◽

Regulatory Protein ◽

Transport Systems ◽

Uptake System ◽

Gene Products ◽

Abc Transport ◽

Insertional Inactivation ◽

Atp Binding Protein

ABSTRACT Streptomyces reticuli has an inducible ATP-dependent uptake system specific for cellobiose and cellotriose. By reversed genetics a gene cluster encoding components of a binding protein-dependent cellobiose and cellotriose ABC transporter was cloned and sequenced. The deduced gene products comprise a regulatory protein (CebR), a cellobiose binding lipoprotein (CebE), two integral membrane proteins (CebF and CebG), and the NH2-terminal part of an intracellular β-glucosidase (BglC). The gene for the ATP binding protein MsiK is not linked to the ceb operon. We have shown earlier that MsiK is part of two different ABC transport systems, one for maltose and one for cellobiose and cellotriose, in S. reticuli and Streptomyces lividans. Transcription of polycistronic cebEFG and bglC mRNAs is induced by cellobiose, whereas the cebR gene is transcribed independently. Immunological experiments showed that CebE is synthesized during growth with cellobiose and that MsiK is produced in the presence of several sugars at high or moderate levels. The described ABC transporter is the first one of its kind and is the only specific cellobiose/cellotriose uptake system of S. reticuli, since insertional inactivation of the cebEgene prevents high-affinity uptake of cellobiose.

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