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

2012 ◽  
Vol 34 (10) ◽  
pp. 1907-1914 ◽  
Author(s):  
Sung-Kwon Lee ◽  
SangJoon Mo ◽  
Joo-Won Suh
Keyword(s):  
Abc Transporter ◽  
Binding Protein ◽  
Streptomyces Coelicolor ◽  
Atp Binding ◽  
Atp Binding Protein

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

2019 ◽  
Vol 8 (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.

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

2010 ◽  
Vol 52 (4) ◽  
pp. 561-566 ◽  
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

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

1998 ◽  
Vol 180 (2) ◽  
pp. 290-295 ◽  
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.

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

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

scholarly journals The Vesicle Transport Protein Vps33p Is an ATP-binding Protein That Localizes to the Cytosol in an Energy-dependent Manner

1998 ◽  
Vol 273 (25) ◽  
pp. 15818-15829 ◽  
Author(s):  
Brenda Gerhardt ◽  
Timothy J. Kordas ◽  
Chad M. Thompson ◽  
Purvi Patel ◽  
Thomas Vida
Keyword(s):  
Binding Protein ◽  
Transport Protein ◽  
Vesicle Transport ◽  
Atp Binding ◽  
Dependent Manner ◽  
Energy Dependent ◽  
Atp Binding Protein

scholarly journals Redundancy in Periplasmic Binding Protein-Dependent Transport Systems for Trehalose, Sucrose, and Maltose in Sinorhizobium meliloti

2002 ◽  
Vol 184 (11) ◽  
pp. 2978-2986 ◽  
Author(s):  
John Beck Jensen ◽  
N. Kent Peters ◽  
T. V. Bhuvaneswari
Keyword(s):  
Nitrogen Fixation ◽  
Sinorhizobium Meliloti ◽  
Binding Protein ◽  
Regulatory Protein ◽  
Gene Replacement ◽  
Transport Systems ◽  
Atp Binding ◽  
Dependent Transport ◽  
Atp Binding Protein ◽  
Growth Experiments

ABSTRACT We have identified a cluster of six genes involved in trehalose transport and utilization (thu) in Sinorhizobium meliloti. Four of these genes, thuE, -F, -G, and -K, were found to encode components of a binding protein-dependent trehalose/maltose/sucrose ABC transporter. Their deduced gene products comprise a trehalose/maltose-binding protein (ThuE), two integral membrane proteins (ThuF and ThuG), and an ATP-binding protein (ThuK). In addition, a putative regulatory protein (ThuR) was found divergently transcribed from the thuEFGK operon. When the thuE locus was inactivated by gene replacement, the resulting S. meliloti strain was impaired in its ability to grow on trehalose, and a significant retardation in growth was seen on maltose as well. The wild type and the thuE mutant were indistinguishable for growth on glucose and sucrose. This suggested a possible overlap in function of the thuEFGK operon with the aglEFGAK operon, which was identified as a binding protein-dependent ATP-binding transport system for sucrose, maltose, and trehalose. The Km s for trehalose transport were 8 ± 1 nM and 55 ± 5 nM in the uninduced and induced cultures, respectively. Transport and growth experiments using mutants impaired in either or both of these transport systems show that these systems form the major transport systems for trehalose, maltose, and sucrose. By using a thuE′-lacZ fusion, we show that thuE is induced only by trehalose and not by cellobiose, glucose, maltopentaose, maltose, mannitol, or sucrose, suggesting that the thuEFGK system is primarily targeted toward trehalose. The aglEFGAK operon, on the other hand, is induced primarily by sucrose and to a lesser extent by trehalose. Tests for root colonization, nodulation, and nitrogen fixation suggest that uptake of disaccharides can be critical for colonization of alfalfa roots but is not important for nodulation and nitrogen fixation per se.

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