RESUMEN
Autodisplay of a multimeric protein complex on a cell surface is limited by intrinsic factors such as the types and orientations of anchor modules. Moreover, improper folding of proteins to be displayed often hinders functional cell surface display. While overcoming these drawbacks, we ultimately extended the applicability of the autodisplay platform to the display of a protein complex. We designed and constructed a cell surface attachment (CSA) system that uses a noncovalent protein-protein interaction. We employed the high-affinity interaction mediated by an orthogonal cohesin-dockerin (Coh-Doc) pair from Archaeoglobus fulgidus to build the CSA system. Then, we validated the orthogonal Coh-Doc binding by attaching a monomeric red fluorescent protein to the cell surface. In addition, we evaluated the functional anchoring of proteins fused with the Doc module to the autodisplayed Coh module on the surface of Escherichia coli. The designed CSA system was applied to create a functional attachment of dimeric α-neoagarobiose hydrolase to the surface of E. coli cells.
Asunto(s)
Proteínas Arqueales/metabolismo , Proteínas de Ciclo Celular/metabolismo , Técnicas de Visualización de Superficie Celular/métodos , Proteínas Cromosómicas no Histona/metabolismo , Secuencia de Aminoácidos , Proteínas Arqueales/química , Proteínas Arqueales/genética , Archaeoglobus fulgidus , Proteínas de Ciclo Celular/química , Proteínas de Ciclo Celular/genética , Membrana Celular/genética , Membrana Celular/metabolismo , Proteínas Cromosómicas no Histona/química , Proteínas Cromosómicas no Histona/genética , Disacaridasas/química , Disacaridasas/genética , Disacaridasas/metabolismo , Escherichia coli/genética , Escherichia coli/metabolismo , Proteínas Luminiscentes/química , Proteínas Luminiscentes/genética , Proteínas Luminiscentes/metabolismo , Unión Proteica , Pliegue de Proteína , Proteínas Recombinantes de Fusión/química , Proteínas Recombinantes de Fusión/genética , Proteínas Recombinantes de Fusión/metabolismo , Proteína Fluorescente Roja , CohesinasRESUMEN
Lactobacillus rhamnosus GG (LGG) is a probiotic commonly used in fermented dairy products. In this study, RNA-sequencing was performed to unravel the effects of acid stress on LGG. The transcriptomic data revealed that the exposure of LGG to acid at pH 4.5 (resembling the final pH of fermented dairy products) for 1 h or 24 h provoked a stringent-type transcriptomic response wherein stress response- and glycolysis-related genes were upregulated, whereas genes involved in gluconeogenesis, amino acid metabolism, and nucleotide metabolism were suppressed. Notably, the pilus-specific adhesion genes, spaC, and spaF were significantly upregulated upon exposure to acid-stress. The transcriptomic results were further confirmed via quantitative polymerase chain reaction analysis. Moreover, acid-stressed LGG demonstrated an enhanced mucin-binding ability in vitro, with 1 log more LGG cells (p < 0.05) bound to a mucin layer in a 96-well culture plate as compared to the control. The enhanced intestinal binding ability of acid-stressed LGG was confirmed in an animal study, wherein significantly more viable LGG cells (≥ 2 log CFU/g) were observed in the ileum, caecum, and colon of acid-stressed LGG-treated mice as compared with a non-acid-stressed LGG-treated control group. To our knowledge, this is the first report showing that acid stress enhanced the intestine-binding ability of LGG through the induction of pili-related genes.
Asunto(s)
Ácidos/farmacología , Adhesión Bacteriana/genética , Intestinos/microbiología , Lacticaseibacillus rhamnosus/efectos de los fármacos , Lacticaseibacillus rhamnosus/fisiología , Transcriptoma/efectos de los fármacos , Regulación hacia Arriba/efectos de los fármacos , Animales , Fimbrias Bacterianas/genética , Lacticaseibacillus rhamnosus/genética , Lacticaseibacillus rhamnosus/metabolismo , Masculino , Ratones , Ratones Endogámicos C57BL , Mucinas/metabolismo , Probióticos , Regulación hacia Arriba/genéticaRESUMEN
Lactic acid is a platform chemical for the sustainable production of various materials. To develop a robust yeast platform for low-pH production of d-lactic acid (LA), an acid-tolerant yeast strain was isolated from grape skins and named Pichia kudriavzevii NG7 by ribosomal RNA sequencing. This strain could grow at pH 2.0 and 50°C. For the commercial application of P. kudriavzevii NG7 as a lactic acid producer, the ethanol fermentation pathway was redirected to lactic acid by replacing the pyruvate decarboxylase 1 gene (PDC1) with the d-lactate dehydrogenase gene (d-LDH) derived from Lactobacillus plantarum. To enhance lactic acid tolerance, this engineered strain was adapted to high lactic acid concentrations, and a new transcriptional regulator, PAR1, responsible for acid tolerance, was identified by whole-genome resequencing. The final engineered strain produced 135 g/L and 154 g/L of d-LA with productivity over 3.66 g/L/hr at pH 3.6 and 4.16 g/L/hr at pH 4.7, respectively.
Asunto(s)
Ácido Láctico/metabolismo , Ingeniería Metabólica/métodos , Pichia/aislamiento & purificación , Pichia/metabolismo , Ácidos/toxicidad , ADN de Hongos/química , ADN de Hongos/genética , ADN Ribosómico/química , ADN Ribosómico/genética , Tolerancia a Medicamentos , Concentración de Iones de Hidrógeno , Redes y Vías Metabólicas/genética , Filogenia , Pichia/clasificación , Pichia/efectos de los fármacos , Análisis de Secuencia de ADN , Temperatura , Vitis/microbiologíaRESUMEN
Pichia kudriavzevii NG7 is a multistress-tolerant yeast, isolated from grape skins. Here, we report the draft genome sequence of P. kudriavzevii NG7, to understand its biochemical regulation and metabolic pathways.
RESUMEN
A global transcriptome analysis of the natural succinate producer Actinobacillus succinogenes revealed that 353 genes were differentially expressed when grown on various carbon and energy sources, which were categorized into six functional groups. We then analyzed the expression pattern of 37 potential C4 -dicarboxylate transporters in detail. A total of six transporters were considered potential fumarate transporters: three transporters, Asuc_1999 (Dcu), Asuc_0304 (DASS), and Asuc_0270-0273 (TRAP), were constitutively expressed, whereas three others, Asuc_1568 (DASS), Asuc_1482 (DASS), and Asuc_0142 (Dcu), were differentially expressed during growth on fumarate. Transport assays under anaerobic conditions with [14 C]fumarate and [14 C]succinate were performed to experimentally verify that A. succinogenes possesses multiple C4 -dicarboxlayte transport systems with different substrate affinities. Upon uptake of 5 mmol/L fumarate, the systems had substrate specificity for fumarate, oxaloacetate, and malate, but not for succinate. Uptake was optimal at pH 7, and was dependent on both proton and sodium gradients. Asuc_1999 was suspected to be a major C4 -dicarboxylate transporter because of its noticeably high and constitutive expression. An Asuc_1999 deletion (∆1999) decreased fumarate uptake significantly at approximately 5 mmol/L fumarate, which was complemented by the introduction of Asuc_1999. Asuc_1999 expressed in Escherichia coli catalyzed fumarate uptake at a level of 21.6 µmol·gDW-1 ·min-1 . These results suggest that C4 -dicarboxylate transport in A. succinogenes is mediated by multiple transporters, which transport various types and concentrations of C4 -dicarboxylates.
Asunto(s)
Actinobacillus/genética , Actinobacillus/metabolismo , Transportadores de Ácidos Dicarboxílicos/genética , Transportadores de Ácidos Dicarboxílicos/metabolismo , Ácidos Dicarboxílicos/metabolismo , Perfilación de la Expresión Génica , Actinobacillus/crecimiento & desarrollo , Anaerobiosis , Radioisótopos de Carbono/metabolismo , Clonación Molecular , Metabolismo Energético , Escherichia coli/genética , Escherichia coli/metabolismo , Fumaratos/metabolismo , Expresión Génica , Concentración de Iones de Hidrógeno , Marcaje Isotópico , Succinatos/metabolismoRESUMEN
Here, we report the draft genome sequence of the acid-tolerant yeast Candida zemplinina NP2, which was isolated from peach peels. This genome sequence will aid in the understanding of the organism's physiological properties as a potential producer of organic acids in acidic environments.
RESUMEN
We report here the draft genome sequence of the lipolytic yeast Candida aaseri SH-14, isolated from the compost of oil palm empty fruit bunches, and the identification of eight putative lipase genes. This genome information will provide the opportunity to produce potential lipases for a variety of industrial applications.
RESUMEN
The atomic structure of a bacterial aryl acylamidase (EC 3.5.1.13; AAA) is reported and structural features are investigated to better understand the catalytic profile of this enzyme. Structures of AAA were determined in its native form and in complex with the analgesic acetanilide, p-acetaminophenol, at 1.70 Å and 1.73 Å resolutions, respectively. The overall structural fold of AAA was identified as an α/ß fold class, exhibiting an open twisted ß-sheet core surrounded by α-helices. The asymmetric unit contains one AAA molecule and the monomeric form is functionally active. The core structure enclosing the signature sequence region, including the canonical Ser-cisSer-Lys catalytic triad, is conserved in all members of the Amidase Signature enzyme family. The structure of AAA in a complex with its ligand reveals a unique organization in the substrate-binding pocket. The binding pocket consists of two loops (loop1 and loop2) in the amidase signature sequence and one helix (α10) in the non-amidase signature sequence. We identified two residues (Tyr(136) and Thr(330)) that interact with the ligand via water molecules, and a hydrogen-bonding network that explains the catalytic affinity over various aryl acyl compounds. The optimum activity of AAA at pH > 10 suggests that the reaction mechanism employs Lys(84) as the catalytic base to polarize the Ser(187) nucleophile in the catalytic triad.
Asunto(s)
Acetaminofén/química , Amidohidrolasas/química , Proteínas Bacterianas/química , Amidohidrolasas/genética , Secuencias de Aminoácidos , Proteínas Bacterianas/genética , Dominio Catalítico , Cristalografía por Rayos X , Escherichia coli/genética , Escherichia coli/metabolismo , Expresión Génica , Enlace de Hidrógeno , Ligandos , Datos de Secuencia Molecular , Unión Proteica , Estructura Secundaria de Proteína , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Alineación de Secuencia , Especificidad por Sustrato , Agua/químicaRESUMEN
The catabolic fate of the major monomeric sugar of red macroalgae, 3,6-anhydro-L-galactose (AHG), is completely unknown in any organisms. AHG is not catabolized by ordinary fermentative microorganisms, and it hampers the utilization of red macroalgae as renewable biomass for biofuel and chemical production. In this study, metabolite and transcriptomic analyses of Vibrio sp., a marine bacterium capable of catabolizing AHG as a sole carbon source, revealed two key metabolic intermediates of AHG, 3,6-anhydrogalactonate (AHGA) and 2-keto-3-deoxy-galactonate; the corresponding genes were verified in vitro enzymatic reactions using their recombinant proteins. Oxidation by an NADP(+) -dependent AHG dehydrogenase and isomerization by an AHGA cycloisomerase are the two key AHG metabolic processes. This newly discovered metabolic route was verified in vivo by demonstrating the growth of Escherichia coli harbouring the genes of these two enzymes on AHG as a sole carbon source. Also, the introduction of only these two enzymes into an ethanologenic E. coli strain increased the ethanol production in E. coli by fermenting both AHG and galactose in an agarose hydrolysate. These findings provide not only insights for the evolutionary adaptation of a central metabolic pathway to utilize uncommon substrates in microbes, but also a metabolic design principle for bioconversion of red macroalgal biomass into biofuels or industrial chemicals.
Asunto(s)
Metabolismo Energético/genética , Escherichia coli/metabolismo , Galactosa/análogos & derivados , Algas Marinas/metabolismo , Vibrio/metabolismo , Organismos Acuáticos/enzimología , Organismos Acuáticos/genética , Organismos Acuáticos/metabolismo , Biocombustibles , Metabolismo de los Hidratos de Carbono , Escherichia coli/genética , Fermentación/genética , Galactosa/metabolismo , Perfilación de la Expresión Génica , Redes y Vías Metabólicas/genética , Algas Marinas/enzimología , Vibrio/enzimología , Vibrio/genéticaRESUMEN
Screening a library of overexpressing mutant alleles of the TATA-binding gene SPT15 yielded two Saccharomyces cerevisiae strains (MRRC 3252 and 3253) with enhanced tolerance to acetic acid. They were also tolerant to propionic acid and hydrogen peroxide. Transcriptome profile analysis identified 58 upregulated genes and 106 downregulated genes in MRRC 3252. Stress- and protein synthesis-related transcription factors were predominantly enriched in the upregulated and downregulated genes respectively. Eight deletion mutants for some of the highly downregulated genes were acetic acid-tolerant. The level of intracellular reactive oxygen species was considerably lessened in MRRC 3252 and 3253 upon exposure to acetic acid. Metabolome profile analysis revealed that intracellular concentrations of 5 and 102 metabolites were increased and decreased, respectively, in MRRC 3252, featuring a large increase of urea and a significant decrease of amino acids. The dur1/2Δmutant, in which the urea degradation gene DUR1/2 is deleted, displayed enhanced tolerance to acetic acid. Enhanced tolerance to acetic acid was also observed on the medium containing a low concentration of amino acids. Taken together, this study identified two SPT15 alleles, nine gene deletions and low concentration of amino acids in the medium that confer enhanced tolerance to acetic acid.
Asunto(s)
Ácido Acético/farmacología , Farmacorresistencia Fúngica/genética , Proteínas de Saccharomyces cerevisiae/genética , Saccharomyces cerevisiae/efectos de los fármacos , Saccharomyces cerevisiae/genética , Proteína de Unión a TATA-Box/genética , Ácido Acético/metabolismo , Alelos , Aminoácidos/metabolismo , Secuencia de Bases , Etanol/metabolismo , Perfilación de la Expresión Génica , Peróxido de Hidrógeno/farmacología , Mutación , Propionatos/farmacología , Especies Reactivas de Oxígeno/metabolismo , Análisis de Secuencia de ARN , Urea/metabolismoRESUMEN
We used culture-dependent and culture-independent methods to extract previously undescribed plasmids harboring tetracycline (TC) resistance genes from activated sludge. The extracted plasmids were transformed into naturally competent Acinetobacter oleivorans DR1 to recover a non-Escherichia coli-based plasmid. The transformed cells showed 80-100-fold higher TC resistance than the wild-type strain. Restriction length polymorphism performed using 30 transformed cells showed four different types of plasmids. Illumina-based whole sequencing of the four plasmids identified three previously unreported plasmids and one previously reported plasmid. All plasmids carried TC resistance-related genes (tetL, tetH), tetracycline transcriptional regulators (tetR), and mobilization-related genes. As per expression analysis, TC resistance genes were functional in the presence of TC. The recovered plasmids showed mosaic gene acquisition through horizontal gene transfer. Membrane fluidity, hydrophobicity, biofilm formation, motility, growth rate, sensitivity to stresses, and quorum sensing signals of the transformed cells were different from those of the wild-type cells. Plasmid-bearing cells seemed to have an energy burden for maintaining and expressing plasmid genes. Our data showed that acquisition of TC resistance through plasmid uptake is related to loss of biological fitness. Thus, cells acquiring antibiotic resistance plasmids can survive in the presence of antibiotics, but must pay ecological costs.
Asunto(s)
Acinetobacter/genética , Farmacorresistencia Bacteriana Múltiple/genética , Plásmidos/aislamiento & purificación , Aguas del Alcantarillado/microbiología , Resistencia a la Tetraciclina/genética , Acinetobacter/aislamiento & purificación , Alcanos/química , Antibacterianos/farmacología , Biodegradación Ambiental , Biopelículas , ADN Bacteriano/genética , Regulación Bacteriana de la Expresión Génica , Transferencia de Gen Horizontal , Estrés Oxidativo , Fenotipo , Polimorfismo de Longitud del Fragmento de Restricción , Percepción de Quorum , Sales (Química)/metabolismo , Análisis de Secuencia de ADN , Tetraciclina/farmacologíaRESUMEN
Plant expansin proteins induce plant cell wall extension and have the ability to extend and disrupt cellulose. In addition, these proteins show synergistic activity with cellulases during cellulose hydrolysis. BsEXLX1 originating from Bacillus subtilis is a structural homolog of a ß-expansin produced by Zea mays (ZmEXPB1). The Langmuir isotherm for binding of BsEXLX1 to microcrystalline cellulose (i.e., Avicel) revealed that the equilibrium binding constant of BsEXLX1 to Avicel was similar to those of other Type A surface-binding carbohydrate-binding modules (CBMs) to microcrystalline cellulose, and the maximum number of binding sites on Avicel for BsEXLX1 was also comparable to those on microcrystalline cellulose for other Type A CBMs. BsEXLX1 did not bind to cellooligosaccharides, which is consistent with the typical binding behavior of Type A CBMs. The preferential binding pattern of a plant expansin, ZmEXPB1, to xylan, compared to cellulose was not exhibited by BsEXLX1. In addition, the binding capacities of cellulose and xylan for BsEXLX1 were much lower than those for CtCBD3.
Asunto(s)
Bacillus subtilis/química , Proteínas Bacterianas/metabolismo , Celulosa/metabolismo , Proteínas de Plantas/química , Bacillus subtilis/enzimología , Proteínas Bacterianas/química , Cationes/química , Celulosa/química , Concentración Osmolar , Unión Proteica , Cloruro de Sodio , Homología Estructural de Proteína , Tensoactivos/químicaRESUMEN
BsEXLX1 from Bacillus subtilis is the first discovered bacterial expansin as a structural homolog of a plant expansin, and it exhibited synergism with cellulase on the cellulose hydrolysis in a previous study. In this study, binding characteristics of BsEXLX1 were investigated using pretreated and untreated Miscanthus x giganteus in comparison with those of CtCBD3, a cellulose-binding domain from Clostridium thermocellum. The amounts of BsEXLX1 bound to cellulose-rich substrates were significantly lower than those of CtCBD3. However, the amounts of BsEXLX1 bound to lignin-rich substrates were much higher than those of CtCBD3. A binding competition assay between BsEXLX1 and CtCBD3 revealed that binding of BsEXLX1 to alkali lignin was not affected by the presence of CtCBD3. This preferential binding of BsEXLX1 to lignin could be related to root colonization in plants by bacteria, and the bacterial expansin could be used as a lignin blocker in the enzymatic hydrolysis of lignocellulose.
Asunto(s)
Bacillus subtilis/metabolismo , Proteínas Bacterianas/metabolismo , Proteínas Portadoras/metabolismo , Lignina/metabolismo , Clostridium thermocellum/metabolismo , Modelos Moleculares , Poaceae/química , Unión Proteica , Conformación ProteicaRESUMEN
The metabolic fate of 3,6-anhydro-L-galactose (L-AHG) is unknown in the global marine carbon cycle. Vibrio sp. strain EJY3 is an agarolytic marine bacterium that can utilize L-AHG as a sole carbon source. To elucidate the metabolic pathways of L-AHG, we have sequenced the complete genome of Vibrio sp. strain EJY3.
Asunto(s)
Galactosa/análogos & derivados , Genoma Bacteriano , Vibrio/clasificación , Vibrio/genética , Galactosa/metabolismo , Datos de Secuencia Molecular , Océanos y Mares , Filogenia , ARN Ribosómico 16S/genética , Microbiología del AguaRESUMEN
A gene, alg7D, from Saccharophagus degradans, coding for a putative alginate lyase belonging to the family of polysaccharide lyase-7, was overexpressed in Escherichia coli. The properties of the recombinant Alg7D were characterized. The enzyme endolytically depolymerized alginate by ß-elimination into oligo-alginates with degrees of polymerization of 2-5. Its activity was maximal at 50°C and pH 7 and was slightly increased in the presence of Na(+). The K(M), V(max), k(cat), and k(cat)/K(M) values were: 3 mg ml(-1), 6.2 U mg(-1), 1.9 × 10(-2) s(-1), and 6.3 × 10(-3) mg(-1 )ml s(-1), respectively.
Asunto(s)
Alteromonadaceae/enzimología , Polisacárido Liasas/genética , Polisacárido Liasas/metabolismo , Alginatos/metabolismo , Alteromonadaceae/genética , Estabilidad de Enzimas , Escherichia coli/genética , Expresión Génica , Ácido Glucurónico/metabolismo , Ácidos Hexurónicos/metabolismo , Concentración de Iones de Hidrógeno , Cinética , Oligosacáridos/metabolismo , Polisacárido Liasas/química , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , TemperaturaRESUMEN
Autotransporters have been employed as the anchoring scaffold for cell surface display by replacing their passenger domains with heterologous proteins to be displayed. We adopted an autotransporter (YfaL) of Escherichia coli for the cell surface display system. The critical regions in YfaL for surface display were identified for the construction of a ligation-independent cloning (LIC)-based display system. The designed system showed no detrimental effect on either the growth of the host cell or overexpressing heterologous proteins on the cell surface. We functionally displayed monomeric red fluorescent protein (mRFP1) as a reporter protein and diverse agarolytic enzymes from Saccharophagus degradans 2-40, including Aga86C and Aga86E, which previously had failed to be functional expressed. The system could display different sizes of proteins ranging from 25.3 to 143 kDa. We also attempted controlled release of the displayed proteins by incorporating a tobacco etch virus protease cleavage site into the C termini of the displayed proteins. The maximum level of the displayed protein was 6.1 × 10(4) molecules per a single cell, which corresponds to 5.6% of the entire cell surface of actively growing E. coli.
Asunto(s)
Proteínas de Escherichia coli/genética , Proteínas de Escherichia coli/metabolismo , Escherichia coli/enzimología , Escherichia coli/genética , Vectores Genéticos , Glicósido Hidrolasas/genética , Glicósido Hidrolasas/metabolismo , Proteínas de Transporte de Membrana/genética , Proteínas de Transporte de Membrana/metabolismo , Alteromonadaceae/enzimología , Alteromonadaceae/genética , Genes Reporteros , Ingeniería Genética/métodos , Genética Microbiana/métodos , Glicósido Hidrolasas/química , Proteínas Luminiscentes/análisis , Proteínas Luminiscentes/genética , Peso Molecular , Proteínas Recombinantes/química , Proteínas Recombinantes/genética , Proteínas Recombinantes/metabolismo , Proteína Fluorescente RojaRESUMEN
Aryl acylamidase (EC 3.5.1.13, AAA) acts on the amide bond between aryl and acyl groups. Whole cells of Escherichia coli overexpressing a novel bacterial AAA synthesized p-acetaminophenol (p-AAP) from p-aminophenol (p-AP, aryl compound) and acetate (acyl donor). Optimum conditions were pH 5.5 and 35°C with 100 mM p-AP and 600 mM sodium acetate in 100 mM sodium phosphate buffer including 1% (v/v) Triton X-100 for 60 h. 13.1 g p-AAP l(-1) was produced with a conversion yield of 87%.
Asunto(s)
Acetaminofén/metabolismo , Amidohidrolasas/metabolismo , Escherichia coli/enzimología , Expresión Génica , Amidohidrolasas/genética , Aminofenoles/metabolismo , Escherichia coli/genética , Concentración de Iones de Hidrógeno , Acetato de Sodio/metabolismo , TemperaturaRESUMEN
In agarolytic microorganisms, α-neoagarobiose hydrolase (NABH) is an essential enzyme to metabolize agar because it converts α-neoagarobiose (O-3,6-anhydro-alpha-l-galactopyranosyl-(1,3)-d-galactose) into fermentable monosaccharides (d-galactose and 3,6-anhydro-l-galactose) in the agarolytic pathway. NABH can be divided into two biological classes by its cellular location. Here, we describe a structure and function of cytosolic NABH from Saccharophagus degradans 2-40 in a native protein and d-galactose complex determined at 2.0 and 1.55 Å, respectively. The overall fold is organized in an N-terminal helical extension and a C-terminal five-bladed ß-propeller catalytic domain. The structure of the enzyme-ligand (d-galactose) complex predicts a +1 subsite in the substrate binding pocket. The structural features may provide insights for the evolution and classification of NABH in agarolytic pathways.
Asunto(s)
Alteromonadaceae/enzimología , Disacaridasas/química , Agar/química , Agar/metabolismo , Clonación Molecular , Citosol/enzimología , Disacaridasas/genética , Conformación ProteicaRESUMEN
Verrucosispora maris AB-18-032 is a marine actinomycete that produces atrop-abyssomicin C and proximicin A, both of which have novel structures and modes of action. In order to understand the biosynthesis of these compounds, to identify further biosynthetic potential, and to facilitate rational improvement of secondary metabolite titers, we have sequenced the complete 6.7-Mb genome of Verrucosispora maris AB-18-032.
Asunto(s)
ADN Bacteriano/química , ADN Bacteriano/genética , Genoma Bacteriano , Micromonosporaceae/genética , Antineoplásicos/metabolismo , Compuestos Bicíclicos Heterocíclicos con Puentes/metabolismo , Micromonosporaceae/aislamiento & purificación , Micromonosporaceae/metabolismo , Datos de Secuencia Molecular , Netropsina/análogos & derivados , Netropsina/metabolismo , Análisis de Secuencia de ADN , Microbiología del AguaRESUMEN
Lactobacillus acidophilus 30SC has been isolated from swine intestines and considered a probiotic strain for dairy products because of its ability to assimilate cholesterol and produce bacteriocins. Here, we report the complete genome sequence of Lactobacillus acidophilus 30SC (2,078,001 bp) exhibiting strong acid resistance and enhanced bile tolerance.