Comaprison of Strains of Streptomyces griseus which produce Streptomycin and those which do not

Szabó, Gábor; Valyi-Nagy, T; Barabás, Gy.; Bássler, G.

doi:10.1038/188428a0

Cited by 14 publications

(10 citation statements)

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“…Cloning in streptomycetes was done in Streptomyces lividans TK64 [7], S. griseus 45H [8] and S. griseus 52‐1 [8], using the cloning vector pIJ702 [7]. For selection of the plasmid, 50 or 5 μg ml −1 thiostrepton was used in solid and in liquid medium, respectively.…”

Section: Methodsmentioning

confidence: 99%

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

Birkó

Schauwecker

Pfennig

et al. 2001

FEMS Microbiology Letters

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Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5--10 mg of biologically fully active protein per liter culture.

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Section: Methodsmentioning

confidence: 99%

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

Birkó

Schauwecker

Pfennig

et al. 2001

FEMS Microbiology Letters

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“…Strains and cultivation: Strains used in these experiments were described earlier (SZAB~ et al 1961, VITLLIS et al 1963. Streptomyces griseus No.…”

Section: Methodsmentioning

confidence: 99%

Changes of protein pattern of Streptomyces griseus strains that characterize differentiation of mycelia in submerged culture

Vitális

Valu

Békési

et al. 1988

J. Basic Microbiol.

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SlOO fractions were isolated from submerged cultures of well conidiating (No. 45H), nonconidiating (No. 52-1) and factor C treated No. 52-1 Streptomyces griseus strains and analyzed by one-dimensional SDS-PAGE. The quantity and synthesis of soluble proteins were examined on densitograms and fluorograms. The evaluation was carried out by a computer aided method. Specific radioactivities of the protein bands were also calculated.Some groups of protein bands were found to be characteristic of the two strains during development. On the other hand densitograms of the two strains could be in part superimposed showing similarities in the position and relative intensity of bands.Most of the soluble proteins were synthesized all over the life-cycle of both strains, although characteristic individual bands appeared or disappeared during differentiation or when the two strains were compared.The protein pattern of SlOO fraction from factor C treated No. 52-1 cultures became similar although not identical, with that of strain No. 45H. Fluorograms showed closer similarities than densitograms. At 40 h. there were certain peaks of specific radioactivity in the factor C treated mycelium which were missing from strain No. 45H of that age, but were expressed later in the 64 h old mycelium.Although the bands obtained by one-dimensional SDS-PAGE did not represent individual proteins, the results shown demonstrate that our method is suitable for the characterization of the process of biochemical differentiation. The quantitative changes of some bands detected by densiometry, fluorography and specific radioactivity may reflect important events of differentiation (Table 1). 1969).27 J. Basic Microbiol. 28 (lQ88) 6

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“…When required for the maintenance of the plasmids, ampicillin (100 Wg ml 31 ) and kanamycin (25 Wg ml 31 ) were added. Cloning in streptomycetes was done in Streptomyces lividans TK64 [7], S. griseus 45H [8] and S. griseus 52-1 [8], using the cloning vector pIJ702 [7]. For selection of the plasmid, 50 or 5 Wg ml 31 thiostrepton was used in solid and in liquid medium, respectively.…”

Section: Materials and Strainsmentioning

confidence: 99%

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+ affinity column chromatography

Birkó¹

2001

FEMS Microbiology Letters

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Factor C is an unusual extracellular protein capable of inducing cytodifferentiation in certain Streptomyces strains. The protein is produced by Streptomyces griseus 45H at such a low amount that the study of its mode of action was hindered by the shortage of purified protein. We report here the expression of C-terminally hexa-His-tagged factor C in Streptomyces lividans and Escherichia coli. Expression in S. lividans is low while in E. coli it is relatively high, yielding about 5^10 mg of biologically fully active protein per liter culture. ß

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Comaprison of Strains of Streptomyces griseus which produce Streptomycin and those which do not

Cited by 14 publications

References 2 publications

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

Changes of protein pattern of Streptomyces griseus strains that characterize differentiation of mycelia in submerged culture

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+ affinity column chromatography

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Comaprison of Strains of Streptomyces griseus which produce Streptomycin and those which do not

Cited by 14 publications

References 2 publications

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+affinity column chromatography

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+affinity column chromatography

Changes of protein pattern of Streptomyces griseus strains that characterize differentiation of mycelia in submerged culture

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni2+ affinity column chromatography

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Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography

Expression and rapid one-step purification of biologically active His-tagged factor C by Ni²⁺affinity column chromatography