Mutants blocked in streptomycin production in Streptomyces griseus - the role of A-factor.

Hara, Osamu; Beppu, Teruhiko

doi:10.7164/antibiotics.35.349

Cited by 181 publications

(115 citation statements)

References 26 publications

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“…The BprA reaction required NADPH but not NADH. Although we did not determine the stereochemistry at position 3 of the A factor produced in this way, its biological activity suggested that almost the entire population of the molecules are the R-form; the 3R-form is essential for A factor activity (19). Thus, A factor is synthesized through not only pathway A but also pathway B.…”

Section: The Downstream Steps In a Factor Biosynthesis After The Afsamentioning

confidence: 88%

“…6C). The extremely low concentration of A factor is still enough for triggering secondary metabolism and morphological development, because exogenous supplementation of A factor at 1 to a few nM is enough to restore streptomycin production of A factor-deficient mutants (19). How is the A factor biosynthesis in such small quantities controlled during the growth?…”

Section: The Variety Of ␥-Butyrolactone Signal Molecules In Streptomymentioning

confidence: 99%

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Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces

Kato¹,

Funa²,

Watanabe

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

168

207

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A factor (2-isocapryloyl-3R-hydroxymethyl-␥-butyrolactone) is a representative of the ␥-butyrolactone autoregulators that trigger secondary metabolism and morphogenesis in the Gram-positive, filamentous bacterial genus Streptomyces. Here, we report the A factor biosynthesis pathway in Streptomyces griseus. The monomeric AfsA, containing a tandem repeat domain of Ϸ80 aa, catalyzed ␤-ketoacyl transfer from 8-methyl-3-oxononanoyl-acyl carrier protein to the hydroxyl group of dihydroxyacetone phosphate (DHAP), thus producing an 8-methyl-3-oxononanoyl-DHAP ester. The fatty acid ester was nonenzymatically converted to a butenolide phosphate by intramolecular aldol condensation. The butenolide phosphate was then reduced by BprA that was encoded just downstream of afsA. The phosphate group on the resultant butanolide was finally removed by a phosphatase, resulting in formation of A factor. The 8-methyl-3-oxononanoyl-DHAP ester produced by the action of AfsA was also converted to A factor in an alternative way; the phosphate group on the ester was first removed by a phosphatase and the dephosphorylated ester was converted nonenzymatically to a butenolide, which was then reduced by a reductase different from BprA, resulting in A factor. Because introduction of afsA alone into Escherichia coli caused the host to produce a substance having A factor activity, the reductase(s) and phosphatase(s) were not specific to the A factor biosynthesis but commonly present in bacteria. AfsA is thus the key enzyme for the biosynthesis of ␥-butyrolactones.A factor ͉ Streptomyces griseus ͉ AfsA ͉ cell-to-cell signaling

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Section: The Downstream Steps In a Factor Biosynthesis After The Afsamentioning

confidence: 88%

Section: The Variety Of ␥-Butyrolactone Signal Molecules In Streptomymentioning

confidence: 99%

Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces

Kato¹,

Funa²,

Watanabe

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

168

207

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“…Martin (1977) summarized the possible candidates: ATP (Silaeva et al, 1965), adenylate energy charge (Atkinson, 1969), polyphosphates (Harold, 1966) or highly phosphorylated nucleotides. Ochi (1987) emphasized the importance of the level of GTP and its hyperphosphorylated derivative, ppGpp (Gallant, 1979), in controlling synthesis of A-factor, and thereby streptomycin production (Hara & Beppu, 1982), in Streptomyces griseus. Our own studies throw no light on the nature of a phosphorylated regulatory molecule in S. coelicolor ; however, recent work by Bibb & Strauch (1990) appears to rule out ppGpp as a candidate.…”

Section: Discussionmentioning

confidence: 99%

Pigmented antibiotic production by Streptomyces coelicolor A3(2): kinetics and the influence of nutrients

Hobbs¹,

Frazer²,

Gardner

et al. 1990

Journal of General Microbiology

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~_ _ _ _ _ _~ _ _ _ _ _ _ _~The production of the pigments actinorhodin and undecylprodigiosin by Stveptomyces coelicolor A3(2) was examined in a chemically defined medium which permits dispersed growth of the organism. The physiological controls on the production of the two pigments were markedly disparate. Actinorhodin production occurred mainly in the stationary phase of batch cultures grown with glucose and sodium nitrate as the principal carbon and nitrogen sources. In the same batch cultures, undecylprodigiosin accumulated during the exponential growth phase. The production of both pigments was sensitive to the levels of ammonium and phosphate in the medium. Actinorhodin production was exquisitely sensitive to ammonium concentration, and was completely inhibited by as little as 1 mM-ammonium chloride, whereas more than 50 mhl-amnonium chloride was required to prevent undecylprodigiosin production. A similar, but less extreme effect was seen with phosphate: actinorhodin production was completely inhibited by 24 mM-phosphate, whereas undecylprodigiosin was still formed at this high phosphate concentration. The effects of ammonium inhibition of pigmented antibiotic production were relieved by reducing the concentration of phosphate in the medium, but changing the ammonium concentration had no effect on phosphate inhibition. Thus the regulation of pigment production by these two nutrients is interrelated, with phosphate control being epistatic to that of ammonium. The results implicate a phosphorylated intermediate as a major regulator of secondary metabolite synthesis by S. coelicolor.

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“…4). In a bioautogram, 2) the Rf values of the active substance produced by each of the transformants were the same as that of chemically synthesized A-factor.1) Usually, A-factor-producing Streptormyces strains obtained from culture collections produce 2 to 5 ng of A-factor per colony, while the above transformants of S. albus IFO 3422, S. albus IFO 3710, S. coelicolor A3(2) IFO 3114, and S. viridochromogenes IFO 12376 produced 150, 120, 90 and 120 ng of A-factor, respectively. Acquisition of A-factor productivity appeared neither to influence the morphological features of the transformants nor to cause production of any antimicrobial substance when Bacillus subtilis ATCC 6633 was used as the indicator strain.…”

Section: Methodsmentioning

confidence: 99%

The cloned Streptomyces bikiniensis A-factor determinant.

Horinouchi¹,

Nishiyama²,

Suzuki³

et al. 1985

J. Antibiot.

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Mutants blocked in streptomycin production in Streptomyces griseus - the role of A-factor.

Cited by 181 publications

References 26 publications

Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces

Biosynthesis of γ-butyrolactone autoregulators that switch on secondary metabolism and morphological development in Streptomyces

Pigmented antibiotic production by Streptomyces coelicolor A3(2): kinetics and the influence of nutrients

The cloned Streptomyces bikiniensis A-factor determinant.

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