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Chapters: Escherichia Coli, Streptococcus, Lactobacillus, Clostridium Difficile, Lactobacillus Reuteri, Candida, Saccharomyces, Bacteroides, Bifidobacterium, Lactobacillus Casei, Bacteroides Fragilis, Peptostreptococcus, Fusobacterium, Current Issues in Intestinal Microbiology, Cytophaga, Fibrobacter Succinogenes. Source: Wikipedia. Pages: 125. Not illustrated. Free updates online. Purchase includes a free trial membership in the publisher's book club where you can select from more than a million books without charge. Excerpt: Bacillus coli communis Escherich 1885 Escherichia coli (commonly abbreviated E. coli; pronounced , named after Theodor Escherich) is a Gram negative rod-shaped bacterium that is commonly found in the lower intestine of warm-blooded organisms (endotherms). Most E. coli strains are harmless, but some, such as serotype O157:H7, can cause serious food poisoning in humans, and are occasionally responsible for product recalls. The harmless strains are part of the normal flora of the gut, and can benefit their hosts by producing vitamin K2, and by preventing the establishment of pathogenic bacteria within the intestine. E. coli are not always confined to the intestine, and their ability to survive for brief periods outside the body makes them an ideal indicator organism to test environmental samples for fecal contamination. The bacteria can also be grown easily and its genetics are comparatively simple and easily-manipulated or duplicated through a process of metagenics, making it one of the best-studied prokaryotic model organisms, and an important species in biotechnology and microbiology. E. coli was discovered by German pediatrician and bacteriologist Theodor Escherich in 1885, and is now classified as part of the Enterobacteriaceae family of gamma-proteobacteria. Model of successive binary fission in E. coliA strain of E. coli is a sub-group within the species that has unique characteristics that distingu...More: http://booksllc.net/?id=40114 ... Read more

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This digital document is a journal article from DNA Repair, published by Elsevier in 2006. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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In Saccharomyces cerevisiae the Rad4-Rad23 complex is involved in initial damage recognition and responsible for recruiting the other NER proteins to the site of the lesion. The Rad4-Rad23 complex is essential for both NER subpathways, Transcription Coupled Repair (TCR) and Global Genome Repair (GGR). Previously, we reported on the role of the Rad4 homologue YDR314C in NER. YDR314C is essential for preferential repair of the transcribed strand in RNA pol I transcribed rDNA. In large scale interaction studies it was shown that YDR314C physically interacts with a small protein encoded by the ORF YML011C. In the present study we show that YML011C is involved in NER and we propose to designate the YML011C ORF RAD33. Cells deleted for RAD33 display intermediate UV sensitivity that is epistatic with NER. Strand specific repair analysis shows that GGR in RNA pol II transcribed regions is completely defective in rad33 mutants whereas TCR is still active, albeit much less efficient. In RNA pol I transcribed rDNA both GGR and TCR are fully dependent on Rad33. We show that in both rad23 and rad33 cells Rad4 and YDR314C protein levels are significantly reduced. The homology of YDR314C to Rad4, together with the similar relation of both proteins to Rad33 prompted us to propose RAD34 as name for the YDR314C gene. Although the rad23rad33 double mutant is considerably more UV sensitive than a rad23 or rad33 single mutant, deletion of RAD33 in a rad23 background does not lead to a further reduction of Rad4 or Rad34 protein levels. This suggests that the role of Rad33 is not solely the stabilization of Rad4 and Rad34 but that Rad33 has an additional role in NER. ... Read more

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High Quality Content by WIKIPEDIA articles! Saccharomyces boulardii is a tropical strain of yeast first isolated from lychee and mangosteen fruit in 1923 by French scientist Henri Boulard. It is related to, but distinct from, Saccharomyces cerevisiae in several taxonomic, metabolic, and genetic properties. S. boulardii has been shown to maintain and restore the natural flora in the large and small intestine; it is classified as a probiotic.S. boulardii is often marketed as a probiotic in a lyophilized form and is therefore often referred to as Saccharomyces boulardii lyo. ... Read more

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This digital document is a journal article from Bioresource Technology, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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A biocatalyst was prepared by immobilizing a commercial Saccharomyces cerevisiae strain (baker's yeast) on orange peel pieces for use in alcoholic fermentation and for fermented food applications. Cell immobilization was shown by electron microscopy and by the efficiency of the immobilized biocatalyst for alcoholic fermentation of various carbohydrate substrates (glucose, molasses, raisin extracts) and at various temperatures (30-15^oC). Fermentation times in all cases were low (5-15h) and ethanol productivities were high (av. 150.6g/ld) showing good operational stability of the biocatalyst and suitability for commercial applications. Reasonable amounts of volatile by-products were produced at all the temperatures studied, revealing potential application of the proposed biocatalyst in fermented food applications, to improve productivities and quality. ... Read more

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This digital document is a journal article from DNA Repair, published by Elsevier in 2005. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Mus81-Mms4/Eme1 is a conserved structure-specific endonuclease that functions in mitotic and meiotic recombination. It has been difficult to identify a single preferred substrate of this nuclease because it is active on a variety of DNA structures. In addition, it has been suggested that the specificity of the recombinant protein may differ from that of the native enzyme. Here, we addressed these issues with respect to Mus81-Mms4 from S. cerevisiae. At low substrate concentrations, Mus81-Mms4 was active on any substrate containing a free end adjacent to the branchpoint. This includes 3'-flap (3'F), regressed leading strand replication fork (RLe), regressed lagging strand replication fork (RLa), and nicked Holliday junction (nHJ) substrates. Kinetic analysis was used to quantitate differences between substrates. High K"c"a"t/K"m values were obtained only for substrates with a 5'-end near the branchpoint (i.e., 3'F, RLe, and nHJ); 10-fold lower values were obtained for nicked duplex (nD) and RLa substrates. Substrates lacking any free ends at the branch point generated K"c"a"t/K"m values that were four orders of magnitude lower than those of the preferred substrates. Native Mus81-Mms4 was partially purified from yeast cells and found to retain its preference for 3'F over intact HJ substrates. Taken together, these results narrow the range of optimal substrates for Mus81-Mms4 and indicate that, at least for S. cerevisae, the native and recombinant enzymes display similar substrate specificities. ... Read more

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This digital document is an article from Revista Científica de la Facultad de Ciencias Veterinarias, published by Thomson Gale on November 1, 2006. The length of the article is 7904 words. The page length shown above is based on a typical 300-word page. The article is delivered in HTML format and is available in your Amazon.com Digital Locker immediately after purchase. You can view it with any web browser.

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Title: Efecto del consumo de cultivo de levadura Saccharomyces [cerevisiae.sup.1026] y/o selenio en pollos de engorde expuestos a bajos niveles de aflatoxina [B.sub.1] en la dieta. 1. Valores de proteinas sericas y actividad enzimatica en suero.
Author: Darwuin Arrieta
Publication: Revista Científica de la Facultad de Ciencias Veterinarias (Magazine/Journal)
Date: November 1, 2006
Publisher: Thomson Gale
Volume: 16Issue: 6Page: 613(9)

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This digital document is a journal article from DNA Repair, published by Elsevier in 2004. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Mitochondrial DNA (mtDNA) is located close to the respiratory chain, a major source of reactive oxygen species (ROS). This proximity makes mtDNA more vulnerable than nuclear DNA to damage by ROS. Therefore, the efficient repair of oxidative lesions in mtDNA is essential for maintaining the stability of the mitochondrial genome. A series of genetic and biochemical studies has indicated that eukaryotic cells, including the model organism Saccharomyces cerevisiae, use several alternative strategies to prevent mutagenesis induced by endogenous oxidative damage to nuclear DNA. However, apart from base excision repair (BER), no other pathways involved in the repair of oxidative damage in mtDNA have been identified. In this study, we have examined mitochondrial mutagenesis in S. cerevisiae cells which lack the activity of the Ogg1 glycosylase, an enzyme playing a crucial role in the removal of 8-oxoG, the most abundant oxidative lesion of DNA. We show that the overall frequency of the mitochondrial oligomycin-resistant (Oli^r) mutants is increased in the ogg1 strain by about one order of magnitude compared to that of the wild-type strain. Noteworthy, in the mitochondrial oli1 gene, G:C to T:A transversions are generated approximately 50-fold more frequently in the ogg1 mutant relative to the wild-type strain. We also demonstrate that the increased frequency of Oli^r mutants in the ogg1 strain is markedly reduced by the presence of plasmids encoding Msh1p, a homologue of the bacterial mismatch protein MutS, which specifically functions in mitochondria. This suppression of the mitochondrial mutator phenotype of the ogg1 strain seems to be specific, since overexpression of the mutant allele msh1-R813W failed to exert this effect. Finally, we also show that the increased frequency of Oli^r mutants arising in an msh1/MSH1 heterozygote grown in glucose-containing medium is further enhanced if the cells are cultivated in glycerol-containing medium, i.e. under conditions when the respiratory chain is fully active. Taken together, these results strongly suggest that MSH1-dependent repair represents a significant back-up to mtBER in the repair of oxidative damage in mtDNA. ... Read more

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This digital document is a journal article from Analytica Chimica Acta, published by Elsevier in . The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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The preparation of chemically functionalized self-assembled monolayer (SAM) surfaces is of great interest for applications in the immobilization of various bioactive species such as enzymes, DNA, whole cells, etc. In this paper, an electrochemical impedance biosensor for the rapid detection of Saccharomyces cerevisiae (yeast cells) was developed by immobilizing yeast cells on a gold surface modified with an alkanethiolate SAM. The patterns formed on the gold electrode surface after the assembly of 3-mercaptopropionic acid (MPA) monolayer and the immobilization of yeast cells were clearly observed from atomic force microscopy (AFM) and optical microscope, respectively. The electrochemical impedance spectroscopy (EIS) measurements were based on the charge-transfer kinetics of [Fe(CN)"6]^3^-^/^4^- redox couple. The SAM assembly and the subsequent immobilization of yeast cells on the gold electrodes greatly increased the electron-transfer resistance (R"e"t) of the redox couple and decreased the double layer capacitance (C"d"l). A linear relationship between the R"e"t and logarithmic value of yeast concentrations was found in the range between 10^2 and 10^8cfumL^-^1. ... Read more

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This digital document is a journal article from Journal of Hazardous Materials, published by Elsevier in 2006. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Mixing patterns and modes have a great influence on the efficiency of biological treatment systems. A series of laboratory experiments was conducted with a controlled, small-scale analog of a pilot wastewater aeration tank, consisting of two eccentrically placed cylinders. By controlling the rotation direction and speed of the two cylinders, it has been possible to develop chaotic flow fields in the space between the walls of the cylinders. Our experiments utilized Saccharomyces cerevisiae as the biological oxidation organism and air bubbles as the mixing agent supplied by a large fine pore diffuser to the cells in their exponential growth phase. The effect of various mixing patterns on cell growth was studied at different cylinder eccentricities, rotation directions and speeds. It was found that chaotic advection flow patterns: (a) enhanced growth, and (b) sped up the onset of maximal growth of the organism by 15-18% and 14-20%, respectively. ... Read more

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This digital document is a journal article from DNA Repair, published by Elsevier in . The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Reactive oxygen species can attack the mitochondrial genome to produce a vast array of oxidative DNA lesions including 8-oxo-7,8-dihydro-2'-deoxyguanosine (8-oxo-dGuo). We assess the role of the Saccharomyces cerevisiae 8-oxo-dGuo DNA glycosylase, Ogg1, in the maintenance of a poly(GT) tract reporter system present in the mitochondrial genome. Deletion in the poly(GT) tract causes the reporter system to produce arginine-independent (Arg^+) colonies. We show that the mitochondrial form of Ogg1 is functionally active at processing 8-oxo-dGuo lesions and that Ogg1-deficient cells exhibit nearly six-fold elevated rate of Arg^+ mutants under normal growth condition, as compared to the parent. Overexpression of Ogg1 completely suppressed the high rate of Arg^+ mutations to levels lower than the parental, suggesting that Ogg1 function could be limited in the mitochondria. Further analysis revealed that the Arg^+ mutations can be prevented if the cells are grown under anaerobic conditions. These findings provide in vivo evidence that oxidative stress induces the formation of lesions, most likely 8-oxo-dGuo, which must be repaired by Ogg1, otherwise the lesions can trigger poly(GT) tract instability in the mitochondrial genome. We also demonstrate that overproduction of the major apurinic/apyrimidinic (AP) endonuclease Apn1, a nuclear and mitochondrial enzyme with multiple DNA repair activities, substantially elevated the rate of Arg^+ mutants, but which was counteracted by Ogg1 overexpression. We suggest that Ogg1 might bind to AP sites and protect this lesion from the spurious action of Apn1 overproduction. Thus, cleavage of AP site located within or in the vicinity of the poly(GT) tract could destabilize this repeat. ... Read more

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The expression of proteins from different host organisms is of big interest in the modern biotechnology. Not only for commercial or medical purposes, but also for the characterization of foreign proteins the heterologous expression plays a significant role.How can a foreign protein be expressed in a pro- or eukaryotic host? Which host is suitable for which kind of protein? How can the specific protein yield be increased by varying process parameter?The author Dr. Falk Matth?us gives introductorily an overview of different host systems for the heterologous expression of proteins. The high cell density fermentation and the applicability of different plasmid systems are discussed in the introduction. The heterologous expression of the putatively celiac disease triggering proteins of the wheat endosperm is the central point of this book. The optimization of fermentation parameter for higher biomass and protein yield are discussed. Furthermore, the adaptation of the classical protein purification to the changed host system as well as the establishment of an aqueous two phase system as alternativ protein purification are discussed. ... Read more

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Ethanol production by yeast fermentation has been infocus of mankind for millennia, initially, asconsumable products like wine and beer, and recentlyas an environmental-friendly fuel. To obtain anefficient industrial production further knowledge ofyeast metabolism is needed to increase the productpurity. In this work, the nitrogen and redoxmetabolism in yeast and its implications on by- product formation and yeast physiology have beenstudied. In this respect, amino acid biosynthesisplays a substantial role and the central amino acid,glutamate, where used as the sole source ofnitrogen. Such cultures were studied in depth bycharacterizing extra- and intracellular metaboliteformation, carbon flows, protein expression andenzyme activities. Glycerol is formed as the main by- product during anaerobic conditions to balance redoxequivalents formed during biosynthesis of mainlyamino acids. Thus, using amino acids as nitrogensource it was found that glycerol formation wasreduced as predicted by theoretical calculations.The results presented in this work have implicationsfor both basic yeast research as well as developmentof yeast bioprocesses. ... Read more

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This digital document is a journal article from DNA Repair, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Trinucleotide repeats (TNRs) frequently expand in certain human genetic diseases, often with devastating pathological consequences. TNR expansions require the addition of new DNA; accordingly, molecular models suggest aberrant DNA replication or error-prone repair synthesis as the sources of most instability. Some proteins are currently known that either promote or inhibit TNR mutability. To identify additional proteins that help protect cells against TNR instability, yeast mutants were isolated with higher than normal rates of CAG.CTG tract expansions. Surprisingly, a rev1 mutant was isolated. In contrast to its canonical function in supporting mutagenesis, we found that Rev1 reduces rates of CAG.CTG repeat expansions and contractions, as judged by the behavior of the rev1 mutant. The rev1 mutator phenotype was specific for TNRs with hairpin forming capacity. Mutations in REV3 or REV7, encoding the subunits of DNA polymerase @z (pol @z), did not affect expansion rates in REV1 or rev1 strains. A rev1 point mutant lacking dCMP transferase activity was normal for TNR instability, whereas the rev1-1 allele that interferes with BRCT domain function was as defective as a rev1 null mutant. In summary, these results indicate that yeast Rev1 reduces mutability of CAG.CTG tracts in a manner dependent on BRCT domain function but independent of dCMP transferase activity and of pol @z. ... Read more

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This digital document is a journal article from Chemosphere, published by Elsevier in 2007. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Saccharomyces cerevisiae MTCC 463 decolourizes toxic azo dye, methyl red by degradation process. Methyl red (100mgl^-^1) is degraded completely within 16min in plain distilled water under static anoxic condition, at the room temperature. Effect of physicochemical parameters (pH of medium, composition of medium, concentration of cells, concentration of dye, temperature and agitation) on methyl red decolourization focused the optimal condition required for decolourization. Biodegradation (fate of metabolism) of methyl red in plain distilled water was found to be pH dependent. Cells of Saccharomyces cerevisiae could degrade methyl red efficiently up to 10 cycles in plain distilled water. Analysis of samples extracted with ethyl acetate from decolourized culture flasks in plain distilled water (pH 6.5) and at pH 9 using UV-VIS, TLC, HPLC and FTIR confirm biodegradation of methyl red into several different metabolites. A study of the enzymes responsible for the biodegradation of methyl red in the control and cells obtained after decolourization in plain distilled water (pH 6.5) and at pH 9 showed different levels of the activities of laccase, lignin peroxidase, NADH-DCIP reductase, azoreductase, tyrosinase and aminopyrine N-demethylase. A significant increase in the activities of lignin peroxidase and NADH-DCIP reductase was observed in the cells obtained after decolourization in plain distilled water (pH 6.5), however cells obtained at pH 9 shows increased activities of azoreductase, tyrosinase, lignin peroxidase and NADH-DCIP reductase. High efficiency to decolourize methyl red in plain distilled water and low requirement of environmental conditions enables this yeast to be used in biological treatment of industrial effluent containing azo dye, methyl red. ... Read more

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This digital document is a journal article from DNA Repair, published by Elsevier in 2006. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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Ionizing radiation-induced mutagenesis (IR-IM) underlies a basis for radiation associated carcinogenesis as well as resistance to radiation therapy. This process was examined in Saccharomyces cerevisiae using an array of isogenic DNA repair deficient mutants. Mutations inactivating homologous recombination (rad51, 52, 54) or nucleotide excision repair (rad1, rad10, rad4) caused elevated IR-IM whereas inactivation of TransLesion Synthesis (TLS: rad6) caused severely defective IR-IM. Of the mutations inactivating TLS polymerases, rev3 and rev1 caused equally severe defects in IR-IM whereas rad30 did not significantly affect the process. The effects of the rev3, rev1, and rad6 mutations on IR-IM were epistatic, suggesting the requirement of both polymerase zeta and Rev1p in IR-IM related TLS. Although PCNA K164 SUMOylation/ubiquitination is a proposed prerequisite for TLS, the IR-IM defect of a rev3 or a rad6 mutant was worse than and epistatic to the pol30K164R mutant, a mutant in which the PCNA had been mutated to abolish such modifications. These results suggested that IR-IM related TLS occurs in the absence of PCNA K164 modification. Further analysis of a mutant simultaneously defective in SUMOylation and mono-ubiquitination (rad18 siz1) revealed that these modifications redundantly affected TLS as well as NHEJ. A genetic model based on these observations is proposed. ... Read more

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This digital document is a journal article from DNA Repair, published by Elsevier in 2004. The article is delivered in HTML format and is available in your Amazon.com Media Library immediately after purchase. You can view it with any web browser.

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High levels of transcription driven by the GAL1-10 promoter stimulate mitotic recombination between direct repeats (DR) as well as between substrates positioned on non-homologous chromosomes. When the substrates are on non-homologous chromosomes, transcription stimulates both gene conversion and crossover events, but the degree of the stimulation varies depending on which substrate is highly transcribed. In gene conversion assays where only one of the substrates is highly transcribed, the effect of transcribing the donor versus the recipient allele can be highly asymmetric. We have examined the basis of this asymmetry and demonstrate that it relates to the nature of the mismatch present in recombination intermediates and the presence of the Msh3 mismatch repair (MMR) protein. In addition to examining the asymmetry conferred by donor versus recipient allele transcription, the possible contribution of transcription elongation problems to transcription-stimulated recombination has been examined using hpr1 mutants. Hpr1 is important for efficient elongation through certain sequences, and in hpr1 mutants, elongation problems have been correlated with elevated recombination between direct repeats. As expected, we found that combining loss of Hpr1 with high levels of transcription had very strong synergistic effects on recombination rates between direct repeats. When the substrates were on non-homologous chromosomes, a weaker synergistic interaction between transcription and Hpr1 loss was observed in gene conversion assays, but only an additive relationship was observed in a crossover-specific assay. Although these data support a causal link between transcription elongation problems and elevated recombination rates, they also indicate that high levels of transcription can stimulate recombination by additional mechanisms. ... Read more