Cloning, sequence and expression of the tyrosinase gene from Streptomyces lavendulae MA406 A-1

Kawamoto, Shinichi; Nakamura, Mitinobu; Yashima, Shigetaka

doi:10.1016/0922-338x(93)90020-9

Cited by 19 publications

(7 citation statements)

References 27 publications

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“…1B ), except for that in S. griseus , in which melD1 and melD2 are separated by 19 bp. In contrast, melC1 and melC2 do not overlap in the known melC operons, except that of S. lavendulae , in which the stop codon of melC1 overlaps the initiation codon of melC2 [24] .…”

Section: Resultsmentioning

confidence: 79%

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Extracellular and Intracellular Polyphenol Oxidases Cause Opposite Effects on Sensitivity of Streptomyces to Phenolics: A Case of Double-Edged Sword

Yang¹,

Chen²

2009

PLoS ONE

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Many but not all species of Streptomyces species harbour a bicistronic melC operon, in which melC2 encodes an extracellular tyrosinase (a polyphenol oxidase) and melC1 encodes a helper protein. On the other hand, a melC-homologous operon (melD) is present in all sequenced Streptomyces chromosomes and could be isolated by PCR from six other species tested. Bioinformatic analysis showed that melC and melD have divergently evolved toward different functions. MelD2, unlike tyrosinase (MelC2), is not secreted, and has a narrower substrate spectrum. Deletion of melD caused an increased sensitivity to several phenolics that are substrates of MelD2. Intracellularly, MelD2 presumably oxidizes the phenolics, thus bypassing spontaneous copper-dependent oxidation that generates DNA-damaging reactive oxygen species. Surprisingly, melC+ strains were more sensitive rather than less sensitive to phenolics than melC − strains. This appeared to be due to conversion of the phenolics by MelC2 to more hydrophobic and membrane-permeable quinones. We propose that the conserved melD operon is involved in defense against phenolics produced by plants, and the sporadically present melC operon probably plays an aggressive role in converting the phenolics to the more permeable quinones, thus fending off less tolerant competing microbes (lacking melD) in the phenolic-rich rhizosphere.

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Section: Resultsmentioning

confidence: 79%

“…Because these species do not produce melanin, these homologs are likely to be melD1 and melD2 . Moreover, Kawamoto et al [24] discovered another melC- hybridizing sequence in melC deletion (Mel − ) mutants of S. lavendulae . This melC homolog is also likely to be a melD operon.…”

Section: Discussionmentioning

confidence: 99%

Extracellular and Intracellular Polyphenol Oxidases Cause Opposite Effects on Sensitivity of Streptomyces to Phenolics: A Case of Double-Edged Sword

Yang¹,

Chen²

2009

PLoS ONE

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“…2 The gene cluster contains 13 open reading frames. Of the 13 gene products, two proteins (GriE and GriF) are similar to the MelC1 and MelC2 proteins, respectively, both of which are responsible for melanin biosynthesis in streptomycetes (17)(18)(19)(20)(21). MelC2 tyrosinase belongs to the type 3 copper protein family, and MelC1 serves as a copper chaperon for MelC2.…”

Section: Resultsmentioning

confidence: 99%

A Novel o-Aminophenol Oxidase Responsible for Formation of the Phenoxazinone Chromophore of Grixazone

Suzuki

Furusho

Higashi

et al. 2006

Journal of Biological Chemistry

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Grixazone contains a phenoxazinone chromophore and is a secondary metabolite produced by Streptomyces griseus. In the grixazone biosynthesis gene cluster, griF (encoding a tyrosinase homolog) and griE (encoding a protein similar to copper chaperons for tyrosinases) are encoded. An expression study of GriE and GriF in Escherichia coli showed that GriE activated GriF by transferring copper ions to GriF, as has been observed for a Streptomyces melanogenesis system in which the MelC1 copper chaperon transfers copper ions to MelC2 tyrosinase. In contrast with tyrosinases, GriF showed no monophenolase activity, although it oxidized various o-aminophenols as preferable substrates rather than catechol-type substrates. Deletion of the griEF locus on the chromosome resulted in accumulation of 3-amino-4-hydroxybenzaldehyde (3,4-AHBAL) and its acetylated compound, 3-acetylamino-4-hydroxybenzaldehyde. GriF oxidized 3,4-AHBAL to yield an o-quinone imine derivative, which was then non-enzymatically coupled with another molecule of the o-quinone imine to form a phenoxazinone. The coexistence of N-acetylcysteine in the in vitro oxidation of 3,4-AH-BAL by GriF resulted in the formation of grixazone A, suggesting that the -SH group of N-acetylcysteine is conjugated to the o-quinone imine formed from 3,4-AHBAL and that the conjugate is presumably coupled with another molecule of the o-quinone imine. GriF is thus a novel o-aminophenol oxidase that is responsible for the formation of the phenoxazinone chromophore in the grixazone biosynthetic pathway.We have long studied the A-factor regulatory cascade that leads to secondary metabolite formation and morphological differentiation in Streptomyces griseus (1, 2). The A-factor (2-isocapryloyl-3R-hydroxymethyl-␥-butyrolactone) triggers the synthesis of almost all the secondary metabolites produced by this species. One of the secondary metabolites under the control of the A-factor is grixazone. Grixazone is a yellow pigment and actually a mixture of grixazones A and B (compounds 1a and 1b) (see Fig. 2C) (3). Grixazone A is a novel compound, and grixazone B has been reported to show a parasiticide activity (4).Grixazones contain a phenoxazinone chromophore. The phenoxazinone skeleton is common to actinomycin D produced by Streptomyces antibioticus (5), michigazone produced by Streptomyces michiganensis (6), texazone produced by Streptomyces sp. WRAT-210 (7), exfoliazone produced by Streptomyces exfoliatus (8), and 4-demethoxymichigazone produced by Streptomyces halstedii (9). Hsieh and Jones (10) reported a phenoxazinone synthase in S. antibioticus that catalyzes the six-electron oxidative coupling of o-aminophenol compounds derived from tryptophan through 3-hydroxyanthranilic acid. However, disruption of the phenoxazinone synthase gene in S. antibioticus does not affect actinomycin D synthesis, showing that the phenoxazinone skeleton in actinomycin D is biosynthesized in vivo by a still unknown enzyme or non-enzymatically (11). On the other hand, michigazone with a hydroxymethyl group at ...

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“…In bacteria, the Streptomyces melanogenesis system has been well studied. In Streptomyces antibioticus , Streptomyces glaucescens and Streptomyces lavendulae , the tyrosinase genes have been cloned, sequenced and shown to encode proteins with identifiable sequence similarity to mammalian tyrosinases (Bernan et al 1985, Huber et al 1985, Kawamoto et al 1993). In other bacterial systems, such as brown‐pigmented strains of Rhizobium leguminosarum b. phaseoli , Azotobacter salinestris and Vibrio tyrosinaticus , melanogenesis has also been studied (Borthakur et al 1987, Ivins and Holmes 1981, Shivprasad and Page 1989).…”

Section: Introductionmentioning

confidence: 99%

Melanin biosynthesis by Frankia strain CeI5

Yuan

Burleigh

Dawson³

2007

Physiologia Plantarum

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Many Frankia strains are pigmented and presumed to produce melanin. However, melanin biosynthesis has yet to be rigorously characterized in Frankia. This study was initiated to determine whether or not Frankia strain CeI5 produced melanin and to identify the biochemical pathway of pigment production. Frankia strain CeI5 first produced a dark pigment in mycelial and other tissue and then in the liquid culture medium when grown in a defined medium containing l-tyrosine. The pigment resisted solvents, lightened when subjected to the action of oxidants, as well as reductants, and produced a flocculent brown precipitate with FeCl(3). Spectroscopic characteristics of the extracted pigment were those of melanin. When subjected to gradual dilution, the absorbance decreased unevenly, occurring in the near red range first, then in the visible range, and lastly in the UV range. This observation might resolve the question of why quite different descriptions of melanin UV-visible light absorption spectra exist in the literature. The tyrosinase cofactor copper greatly enhanced melanin biosynthesis at 5.3 x 10(-6) M, while 1 x 10(-8) M 3,4-dihydroxy-l-phenylalanine hastened pigmentation. The copper-chelating agent KCN and the tyrosinase inhibitor tropolone decreased melanin production at the same concentration of 1 x 10(-5) M. This evidence suggests that Frankia strain CeI5 produces melanin via the Raper and Mason pathway.

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Cloning, sequence and expression of the tyrosinase gene from Streptomyces lavendulae MA406 A-1

Cited by 19 publications

References 27 publications

Extracellular and Intracellular Polyphenol Oxidases Cause Opposite Effects on Sensitivity of Streptomyces to Phenolics: A Case of Double-Edged Sword

Extracellular and Intracellular Polyphenol Oxidases Cause Opposite Effects on Sensitivity of Streptomyces to Phenolics: A Case of Double-Edged Sword

A Novel o-Aminophenol Oxidase Responsible for Formation of the Phenoxazinone Chromophore of Grixazone

Melanin biosynthesis by Frankia strain CeI5

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