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Investigations into biotransformations of unnatural substrates using engineered Streptomyces coelicolorGillan, Rebecca January 2005 (has links)
No description available.
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Selective isolation and characterisation of novel members of thefamily StreptomycetaceaeMeza, Carlos Alberto RodriÌguez January 2004 (has links)
No description available.
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The Streptomyces violaceoruber clade : a model system for defining a post-genomic species concept for streptomycetesKim, Wonyong January 2004 (has links)
No description available.
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The penicillin binding proteins of Streptomyces coelicolorMcCulloch, Louise January 2005 (has links)
No description available.
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Resistance to daptomycin and study of cell wall-related proteins in Streptomyces coelicolorJung, Yong-Gyun January 2007 (has links)
No description available.
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The DNA ligases and associated repair proteins of Streptomyces coelicolorSayer, Heather Rachel January 2008 (has links)
No description available.
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Genetic and biochemical characterisation of Streptomyces coelicolor sigma factor, δм, and its regulator, RsmAGaskell, Alisa A. January 2006 (has links)
No description available.
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Crystallographic studies on polynucleotide phosphorylase from Streptomyces antibioticusSymmons, Martyn Francis January 2004 (has links)
No description available.
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biosystematics of alkaiphilic streptomycetes isolated from a beach and dune sand systemantony-babu, sanjay January 2008 (has links)
Large numbers of alkaliphihc streptomycetes were isolated from six out of seven composite sand samples collected across a beach and sand dune system using starch-casein-nitrate agar supplemented with cycloheximide and buffered to pH 10.5. The isolates, which had colonial and chemotaxonomic properties consistent with their classification in the genus Streptomyces, were assigned to 49 multimembered and 114 single-membered colour-groups given their ability to produce pigments on oatmeal and peptone-yearst- extract agars, and to corresponding groups based on whole-genome rep-PCR banding patterns.
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Investigation of Streptomyces coelicolor A3(2) glycosylation mutantsVarghese, Anpu Susan January 2008 (has links)
This project has established that glycosylation is important for the normal, vegetative growth of <i>S. coelicolor</i>. Three genes SCO3154/<i>pmt, </i>SCO1423/<i>ppm1</i> and a putative SCO1014/<i>ppm2</i> have been identified to be part of the pathway that carries out glycosylation in general, as well as for glycosylation of a phage (πC31cδ25) receptor. The three genes encode protein mannosyltransferase, Pmt and polyprenol phosphate mannose synthases, Ppm1, and Ppm2. Of the three, Ppm2 was previously uncharacterised. Radiolabelling experiments have shown that Ppm1 and Ppm2 are essential for the synthesis of C<sub>45</sub> polyprenol phosphate mannose (Ppm) in <i>S. coelicolor.</i> In collaboration with researchers at Imperial College, London, we have characterised the endogenous polyprenol in <i>S. coelicolor,</i> shown that it consists of nine polyprenol units (C<sub>45</sub>) and provided evidence for the transfer of mannose from GDP-mannose to C<sub>45</sub> polyprenol phosphate. The transfer of mannose to polyprenol phosphates can be inhibited by the addition of amphomycin. The <i>pmt</i> mutant has been shown to contain C<sub>45</sub>-Ppm which implies that the role of Pmt is further down the glycosylation pathway. Glycosylation mutants in <i>ppm1, ppm2</i> and <i>pmt</i> were hypersensitive to rifampicin and cell wall acting drugs, bacitracin and tunicamycin. The <i>ppm1</i> and <i>ppm2</i> mutants were hypersensitive to vancomycin. The MIC of vancomycin for a putative <i>ppm2</i> mutant was between 10-20 μg ml<sup>-1</sup> whereas the WT was resistant to vancomycin at >200 μg ml<sup>-1</sup>. Phage resistance and small colony phenotype can be complemented; antibiotic sensitivities were partially complemented.
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