Characterization of intracellular polysaccharides of <i>Streptomyces</i>

Braña, Alfredo F.; Manzanal, Manuel B.; Hardisson, Carlos

doi:10.1139/m82-197

Cited by 21 publications

(18 citation statements)

References 9 publications

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“…The resulting strain, bkdA1B1C1::aac(3)IV was tested for growth on valine, leucine, or isoleucine as sole carbon source, with growth on alanine as a control, as well as on a medium containing no carbon source. S. coelicolor spores store carbon in the form of trehalose and glycogen [1,9] and are capable of germinating in liquid medium without a carbon source. As shown in Fig.…”

Section: Resultsmentioning

confidence: 99%

Branched-chain amino acid catabolism provides precursors for the Type II polyketide antibiotic, actinorhodin, via pathways that are nutrient dependent

Stirrett

Denoya

Westpheling

2008

J Ind Microbiol Biotechnol

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Polyketide antibiotics are among the most important therapeutics used in human and animal health care. Type II polyketides are composed primarily of acetate-derived thioesters, and the subunits for the PKS are contained in a single module that includes a ketosynthase, acyl carrier protein, chain-length factor and sometimes a keto-reductase, aromatase, cyclase and modifying enzymes, such as glycosylases or hydroxylases. While the enzyme complexes that make up the PKS have been the focus of intense study (Khosla in Chem Rev 7:2577-2590, 1997), the pathways for precursor synthesis have not been established and predictions are complicated by the fact that acetate may be derived from a number of metabolic pathways. Here we show that 50% of the acetate for synthesis of the Type II polyketide, actinorhodin, in Streptomyces coelicolor, is derived from the catabolism of the branched amino acids by pathways that are nutrient dependent. The streptomycetes are apparently unique in that they contain two BCDH gene clusters, each of which is potentially capable of converting leucine, valine and isoleucine to the corresponding thioesters, and contain at least three different pathways for valine catabolism that are differentially used in response to nutrient availability.

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Section: Resultsmentioning

confidence: 99%

Branched-chain amino acid catabolism provides precursors for the Type II polyketide antibiotic, actinorhodin, via pathways that are nutrient dependent

Stirrett

Denoya

Westpheling

2008

J Ind Microbiol Biotechnol

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“…The amount of intracellular glycogen in C. glutamicum was assayed by hydrolysis with amyloglucosidase (Brana et al, 1982). For this purpose, samples (200 ml) of crude cell extracts (prepared as described above) were mixed with 2 vols 97 % (v/v) ethanol, pelleted and redissolved with heating in the same volume of 10 mM sodium/potassium phosphate buffer pH 6?0.…”

Section: Methodsmentioning

confidence: 99%

Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition

et al. 2003

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The analysis of the available Corynebacterium genome sequence data led to the proposal of the presence of all three known pathways for trehalose biosynthesis in bacteria, i.e. trehalose synthesis from UDP-glucose and glucose 6-phosphate (OtsA-OtsB pathway), from malto-oligosaccharides or α-1,4-glucans (TreY-TreZ pathway), or from maltose (TreS pathway). Inactivation of only one of the three pathways by chromosomal deletion did not have a severe impact on C. glutamicum growth, while the simultaneous inactivation of the OtsA-OtsB and TreY-TreZ pathway or of all three pathways resulted in the inability of the corresponding mutants to synthesize trehalose and to grow efficiently on various sugar substrates in minimal media. This growth defect was largely reversed by the addition of trehalose to the culture broth. In addition, a possible pathway for glycogen synthesis from ADP-glucose involving glycogen synthase (GlgA) was discovered. C. glutamicum was found to accumulate significant amounts of glycogen when grown under conditions of sugar excess. Insertional inactivation of the chromosomal glgA gene led to the failure of C. glutamicum cells to accumulate glycogen and to the abolition of trehalose production in a ΔotsAB background, demonstrating that trehalose production via the TreY-TreZ pathway is dependent on a functional glycogen biosynthetic route. The trehalose-non-producing mutant with inactivated OtsA-OtsB and TreY-TreZ pathways displayed an altered cell wall lipid composition when grown in minimal broth in the absence of trehalose. Under these conditions, the mutant lacked both major trehalose-containing glycolipids, i.e. trehalose monocorynomycolate and trehalose dicorynomycolate, in its cell wall lipid fraction. The results suggest that a dramatically altered cell wall lipid bilayer of trehalose-less C. glutamicum mutants may be responsible for the observed growth deficiency of such strains in minimal medium. The results of the genetic and physiological dissection of trehalose biosynthesis in C. glutamicum reported here may be of general relevance for the whole phylogenetic group of mycolic-acid-containing coryneform bacteria.

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“…All determinations were done in triplicate using three independent plates for each time point over the course of differentiation. Extraction and determination of polysaccharides were done as described by Braiia et al (1982), except that the amount of polysaccharides was expressed as pg polysaccharides (mg protein)-' in the cell extract. This expression is more precise since it takes into account only disrupted cells.…”

Section: H O M E R O V a A N D O T H E R Smentioning

confidence: 99%

Disruption of a glycogen-branching enzyme gene, glgB, specifically affects the sporulation-associated phase of glycogen accumulation in Streptomyces aureofaciens

et al. 1996

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~~~In the course of Sfrepfomyces differentiation, glycogen is accumulated in two discrete phases: in substrate hyphae that undergo aerial mycelium formation (phase I), and during septation of aerial hyphae (phase 11). We have disrupted a previously identified gene, g/gB, encoding a putative glycogen-branching enzyme in Streptomyces aureofaciens. Disruption of the gene had no profound effect on sporulation. However, the amount of glycogen-like polysaccharides, compared to wild-type (WT) S-aureofaciens, decreased in the late stage of differentiation of the glgB-disrupted strain. Absorption spectra of polysaccharides extracted from the WT and g/gB-disrupted strains have shown the presence of glycogen in both strains in the first stage of differentiation (aerial mycelium formation), and unbranched glucan was detected in the g/gBdisrupted strain in the late stage of differentiation. The results were confirmed by electron microscopy after silver proteinate staining of glycogen granules. Two distinct glycogen-branching enzymes, which had temporally different expression during differentiation, were detected in WT 5. aureofaciens. The absence of this enzyme activity in the late stage of differentiation in the g/gB mutant suggests that the product of the g/gB gene is responsible for phase II glycogen accumulation.

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Characterization of intracellular polysaccharides of Streptomyces

Cited by 21 publications

References 9 publications

Branched-chain amino acid catabolism provides precursors for the Type II polyketide antibiotic, actinorhodin, via pathways that are nutrient dependent

Branched-chain amino acid catabolism provides precursors for the Type II polyketide antibiotic, actinorhodin, via pathways that are nutrient dependent

Genetic dissection of trehalose biosynthesis in Corynebacterium glutamicum: inactivation of trehalose production leads to impaired growth and an altered cell wall lipid composition

Disruption of a glycogen-branching enzyme gene, glgB, specifically affects the sporulation-associated phase of glycogen accumulation in Streptomyces aureofaciens

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