Sequence of a staphylococcal plasmid gene, vga, encoding a putative ATP-binding protein involved in resistance to virginiamycin A-like antibiotics

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.

Download Full-text

Peer Review #3 of "Characterization of the ATPase FlaI of the motor complex of the Pyrococcus furiosus archaellum and its interactions between the ATP-binding protein FlaH (v0.1)"

10.7287/peerj.4984v0.1/reviews/3 ◽

2018 ◽

Keyword(s):

Peer Review ◽

Pyrococcus Furiosus ◽

Binding Protein ◽

Atp Binding ◽

Motor Complex ◽

Atp Binding Protein

Download Full-text

Genetic and Biochemical Characterization of a High-Affinity Betaine Uptake System (BusA) in Lactococcus lactisReveals a New Functional Organization within Bacterial ABC Transporters

Journal of Bacteriology ◽

10.1128/jb.181.20.6238-6246.1999 ◽

1999 ◽

Vol 181 (20) ◽

pp. 6238-6246 ◽

Cited By ~ 69

Author(s):

David Obis ◽

Alain Guillot ◽

Jean-Claude Gripon ◽

Pierre Renault ◽

Alexander Bolotin ◽

...

Keyword(s):

Abc Transporters ◽

Biochemical Characterization ◽

Transmembrane Domain ◽

Functional Organization ◽

Binding Protein ◽

Atp Binding ◽

Uptake System ◽

High Affinity ◽

Atp Binding Protein

ABSTRACT The cytoplasmic accumulation of exogenous betaine stimulates the growth of Lactococcus lactis cultivated under hyperosmotic conditions. We report that L. lactis possesses a single betaine transport system that belongs to the ATP-binding cassette (ABC) superfamily of transporters. Through transposon mutagenesis, a mutant deficient in betaine transport was isolated. We identified two genes, busAA and busAB, grouped in an operon, busA (betaine uptake system). The transcription of busA is strongly regulated by the external osmolality of the medium. The busAA gene codes for the ATP-binding protein. busAB encodes a 573-residue polypeptide which presents two striking features: (i) a fusion between the regions encoding the transmembrane domain (TMD) and the substrate-binding domain (SBD) and (ii) a swapping of the SBD subdomains when compared to the Bacillus subtilisbetaine-binding protein, OpuAC. BusA of L. lactis displays a high affinity towards betaine (Km = 1.7 μM) and is an osmosensor whose activity is tightly regulated by external osmolality, leading the betaine uptake capacity ofL. lactis to be under dual control at the biochemical and genetic levels. A protein presenting the characteristics predicted for BusAB was detected in the membrane fraction of L. lactis. The fusion between the TMD and the SBD is the first example of a new organization within prokaryotic ABC transporters.

Download Full-text

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.

Download Full-text

The early-onset torsion dystonia gene (DYT1) encodes an ATP-binding protein

Nature Genetics ◽

10.1038/ng0997-40 ◽

1997 ◽

Vol 17 (1) ◽

pp. 40-48 ◽

Cited By ~ 704

Author(s):

Laurie J. Ozelius ◽

Jeffrey W. Hewett ◽

Curtis E. Page ◽

Susan B. Bressman ◽

Patricia L. Kramer ◽

...

Keyword(s):

Early Onset ◽

Binding Protein ◽

Atp Binding ◽

Torsion Dystonia ◽

Atp Binding Protein

Download Full-text

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

Download Full-text

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

Applied and Environmental Microbiology ◽

10.1128/aem.03442-16 ◽

2017 ◽

Vol 83 (7) ◽

Cited By ~ 1

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.

Download Full-text