Search results for "Streptomyce"

Differential proteomic analysis of an engineered Streptomyces coelicolor strain reveals metabolic pathways supporting growth on n-hexadecane

2012

The alkB gene, encoding an alkane monooxygenase in the actinomycete Gordonia sp. SoCg, was expressed in the non-alkane-degrading actinomycete Streptomyces coelicolor M145. The resulting engineered strain, M145-AH, can grow on n-hexadecane as sole carbon source. To unravel proteins associated with growth on n-alkanes, proteome of M145-AH after 6, 24, and 48 h of incubation in the Bushnell-Haas (BH) mineral medium containing n-hexadecane as sole carbon source (H condition) and in BH without any carbon source (0 condition) were compared using 2D-differential gel electrophoresis. Proteome analysis revealed significant changes only at 48 h, showing 48 differentially abundant proteins identified …

La small protein TrpM è coinvolta nel differenziamento morfo-fisiologico di Streptomyces coelicolor

THE SMALL PROTEIN SCO2038 CONTROLS TRYPTOPHAN BIOSYNTHESIS AND DIFFERENTIATION IN STREPTOMYCES COELICOLOR

The cellular regulatory factors comprise regulatory proteins, small RNA and small proteins. It is known that the product of small orfs (smorfs) can regulate the translation of downstream elements and also can encode functional peptides involved in the regulation of specific pathways (Ladoukakis E. et al.,2011). In particular, in the model streptomycete Sfreptomyces coelicolor, smorfs (about 100-300 nucleotides) were identified in some amino acid biosynthetic gene clusters such as in the tryptophan trpCXBA locus (Limauro D. et al., I 990; Hu DS. et al., 1999). In S. coelicolor the molecular mechanisms that regulate tryptophan (Trp) biosynthesis are poorly understood and, unlike the trp opero…

The Histidinol Phosphate Phosphatase Involved in Histidine Biosynthetic Pathway Is Encoded by SCO5208 (hisN) in Streptomyces coelicolor A3(2)

2008

Through the screening of a Streptomyces coelicolor genomic library, carried out in a histidinol phosphate phosphatase (HolPase) deficient strain, SCO5208 was identified as the last unknown gene involved in histidine biosynthesis. SCO5208 is a phosphatase, and it can restore the growth in minimal medium in this HolPase deficient strain when cloned in a high or low copy number vector. Moreover, it shares sequence homology with other HolPases recently identified in Actinobacteria. During this work a second phosphatase, SCO2771, sharing no homologies with SCO5208 and all so far described phosphatases was identified. It can complement HolPase activity mutation only at high copy number. Sequence …

Streptomyces coelicolor extracellular vesicles

This study may reveal the importance of extracellular vesicles in the physiology of S. coelicolor and may also have important biotechnological implications.

Improvement of actinorhodin production yield in Streptomyces coelicolor by immobilized-cell cultivations by using PCL- and PLA-based films

2016

Actinomycetes are Gram-positive bacteria producing most of naturally occurring antibiotics (Donadio et al., 2010). At industrial level, antibiotics are produced by submerged fermentations where the actinomycete filamentous morphology negatively affects bioproductivity (van Dissel et al., 2014). Microporous membranes for bacterial cell-immobilization were already proven increasing bioproductivity in Streptomyces coelicolor, that is a model actinomycete producing the blue pigmented actinorhodin (ACT) antibiotic (Scaffaro et al., 2016). To develop an immobilized-cell bioreactor system, different kinds of polycaprolactone (PCL) and polylactic acid (PLA) films were produced by an electrospinning…

Actinorhodin production intensification by nanofibrous membranes in Streptomyces coelicolor cultures

2016

In this work, electrospun polycaprolactone (PCL) and polylactic acid (PLA) membranes, subjected or not to O2-plasma treatment, werwe used as support for cell-immobilization in S. coelicolor immobilized-cells created a compact biofilm on both kinds of membranes.

Tryptophan promotes morphological and physiological differentiation in Streptomyces coelicolor.

2015

The molecular mechanisms regulating tryptophan biosynthesis in actinomycetes are poorly understood; similarly, the possible roles of tryptophan in the differentiation program of microorganism life-cycle are still underexplored. To unveil the possible regulatory effect of this amino acid on gene expression, an integrated study based on quantitative teverse transcription-PCR (qRT-PCR) and proteomic approaches was performed on the actinomycete model Streptomyces coelicolor. Comparative analyses on the microorganism growth in a minimal medium with or without tryptophan supplementation showed that biosynthetic trp gene expression in S. coelicolor is not subjected to a negative regulation by the …

Pyrocoll, an Antibiotic, Antiparasitic and Antitumor Compound Produced by a Novel Alkaliphilic Streptomyces Strain

2003

A new secondary metabolite was detected in the culture extract of Streptomyces sp. AK 409 by HPLC-diode-array screening. The metabolite was identified as pyrocoll, which is known to be a constituent of cigarette smoke. Pyrocoll is known as a synthetic compound, but until now had not been isolated as a natural product from a microorganism. The compound showed biological activity against various Arthrobacter strains, filamentous fungi, several pathogenic protozoa, and some human tumor cell lines.

Dimer-tetramer transition between solution and crystalline states of streptavidin and avidin mutants.

2003

ABSTRACT The biotin-binding tetrameric proteins, streptavidin from Streptomyces avidinii and chicken egg white avidin, are excellent models for the study of subunit-subunit interactions of a multimeric protein. Efforts are thus being made to prepare mutated forms of streptavidin and avidin, which would form monomers or dimers, in order to examine their effect on quaternary structure and assembly. In the present communication, we compared the crystal structures of binding site W→K mutations in streptavidin and avidin. In solution, both mutant proteins are known to form dimers, but upon crystallization, both formed tetramers with the same parameters as the native proteins. All of the intersub…