Calcium-dependent Bacteriophage DNA Infection

Mandel, M.; Higa, Akiko

doi:10.1016/b978-0-12-131200-8.50033-2

Cited by 231 publications

(228 citation statements)

References 12 publications

Supporting

Mentioning

213

Contrasting

Unclassified

Order By: Relevance

“…DNA fragments were isolated from agarose gels with the Geneclean I1 kit according to the recommendations of the supplier. Transformation of E. coli with plasmid DNA was performed by the CaCl, procedure (Mandel and Higa, 1970).…”

Section: Methodsmentioning

confidence: 99%

4‐Hydroxybenzoate Hydroxylase from Pseudomonas Sp. CBS3

Seibold

Matthes

Eppink

et al. 1996

European Journal of Biochemistry

View full text Add to dashboard Cite

Technical University Hamburg-Harburg, Hamburg, Germany 4-Hydroxybenzoate hydroxylase from Pseudomonus sp. CBS3 was purified by five consecutive steps to apparent homogeneity. The enrichment was 50-fold with a yield of about 20%. The enzyme is a homodimeric flavoprotein monooxygenase with each 44-kDa polypeptide chain containing one FAD molecule as a rather weakly bound prosthetic group. In contrast to other 4-hydroxybenzoate hydroxylases of known primary structure, the enzyme preferred NADH over NADPH as electron donor. The pH optimum for catalysis was pH 8.0 with a maximum turnover rate around 45°C. Chloride ions were inhibitory, and competitive with respect to NADH.4-Hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3 has a narrow substrate specificity. In addition to the transformation of 4-hydroxybenzoate to 3,4-dihydroxybenzoate, the enzyme converted 2-tluoro-4-hydroxybenzoate, 2-cliloro-4-hydroxybenzoate, and 2,4-dihydroxybenzoate. With all aromatic substrates, no uncoupling of hydroxylation was observed.The gene encoding 4-hydroxybenzoate hydroxylase from Pseudomonas sp. CBS3 was cloned in Escherichia coli. Nucleotide sequence analysis revealed an open reading frame of 11 82 bp that corresponded to a protein of 394 amino acid residues. Upstream of the pobA gene, a sequence resembling an E. coli promotor was identified, which led to constitutive expression of the cloned gene in E. coli TG1 . The deduced amino acid sequence of Pseudomanus sp. CBS3 4-hydroxybenzoate hydroxylase revealed 53 % identity with that of the pobA enzyme from Pseudomonasfluorescens for which a three-dimensional structure is known. The active-site residues and the fingerprint sequences associated with FAD binding are strictly conserved. This and the conservation of secondary structures implies that the enzymes share a similar three-dimensional fold. Based on an isolated region of sequence divergence and site-directed mutagenesis data of 4-hydroxybenzoate hydroxylase from f? ,fluorescens, it is proposed that helix H2 is involved in determining the coenzyme specificity.

show abstract

Section: Methodsmentioning

confidence: 99%

4‐Hydroxybenzoate Hydroxylase from Pseudomonas Sp. CBS3

Seibold

Matthes

Eppink

et al. 1996

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…Noteworthy, there are examples of positive influence of surfactants on transformation of bacterial cells due to the resealing the electropermeabilized cells. For these reason, the electroporation was used to make bacteria competent [75].…”

Section: Effect Of Surfactants On Dna Transformationmentioning

confidence: 99%

Structural, biocomplexation and gene delivery properties of hydroxyethylated gemini surfactants with varied spacer length

Zakharova

Gabdrakhmanov

Ibragimova

et al. 2016

Colloids and Surfaces B: Biointerfaces

View full text Add to dashboard Cite

“…Ykast transformations were done by the one-step alkalication method described by Chen et a1.(1992). Bacterial transformations were carried out as described by Mandel and Higa (1970).…”

Section: Manipulation Of Dna and Transformationsmentioning

confidence: 99%

Cloning of two related genes encoding the 56‐kDa and 123‐kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae

Vuorio¹,

Kalkkinen

Londesborough³

1993

European Journal of Biochemistry

143

127

View full text Add to dashboard Cite

Preparations of intact trehalose synthase contain three polypeptides with molecular masses of 56, 102 and 123 kDa. We have cloned the genes TSSl and TSLl coding for the 56-and 123-kDa subunits, respectively. These genes are located on chromosomes I1 (TSSI) and XI11 (TSLI). The TSSl gene was found to be identical with ClFl, a gene required for normal growth on glucose. The product of the entire TSSl gene exibits 37% identity with a 502-amino-acid stretch from the middle of the TSLl product. Disruption of the TSSl gene in yeast eliminates both trehalose 6-phosphate synthase (Tre6P synthase) and trehalose 6-phosphate phosphatase (Tre6Pase) activities, and reintroduction of this gene restores these activities. Transformation of Escherichia coli with TSSl increases its Tre6P synthase activity. Specific proteolytic degradation of the 123-kDa polypeptide from the N-terminus greatly influences the Tre6P synthase activity, decreasing its inhibition by phosphate and activatability by fructose 6-phosphate but has little effect on the Tre6Pase activity. These results suggest that this N-terminal part confers regulatory properties upon the Tre6P synthase activity.Trehalose, a non-reducing disaccharide of glucose, occurs in Saccharomyces cerevisiae during periods of reduced growth, such as during starvation of cells for nitrogen, phosphate or sulfur, as well as during the stationary phase after growth on glucose (Lillie and Pringle, 1980). It is also accumulated in cells exposed to extremes of temperature, dehydration or hazardous chemicals (Attfield, 1987 ;Hottiger et al., 1987;Hino et al., 1990). Experiments using mutants producing varying amounts of trehalose and the increases in intracellular trehalose concentration caused by heat-shock treatment, have shown that heat tolerance, as well as desiccation tolerance, are closely related to the trehalose content of the yeast cell (Hottiger et al., 1987).The formation of trehalose is catalysed by the sequential action of trehalose-6-phosphate synthase (Tre6P synthase) and trehalose-6-phosphate phosphatase (Tre6Pase) activities. These activities co-elute through several chromatographic procedures, suggesting that they are part of a single bifunctional protein (Vandercammen et al., 1989 ;Londesborough and Vuorio, 1991). A protein complex, called trehalose synthase, has been purified in a specifically proteolysed form (Londesborough and Vuorio, 1991) and an apparently intact form (Vuorio et al

show abstract

Calcium-dependent Bacteriophage DNA Infection

Cited by 231 publications

References 12 publications

4‐Hydroxybenzoate Hydroxylase from Pseudomonas Sp. CBS3

4‐Hydroxybenzoate Hydroxylase from Pseudomonas Sp. CBS3

Structural, biocomplexation and gene delivery properties of hydroxyethylated gemini surfactants with varied spacer length

Cloning of two related genes encoding the 56‐kDa and 123‐kDa subunits of trehalose synthase from the yeast Saccharomyces cerevisiae

Contact Info

Product

Resources

About