A trans-acting gene is required for the phenotypic expression of a tyrosinase gene in Streptomyces

Yan Hwa Wu Lee*, Bin Fang Chen, Shwu Yuan Wu, Wei Ming Leu, Jin Jer Lin, Carton W. Chen, Szecheng J. Lo

*Corresponding author for this work

Research output: Contribution to journalJournal Article peer-review

43 Scopus citations


The melanin locus (melC) from Streptomyces antibioticus was previously shown to be composed of two open reading frames (ORFs), melC1 and melC2. The melC2 ORF codes for the polypeptide chain of tyrosinase (apotyrosinase). The function of melC1 is not known except that insertional mutation within it abolishes the tyrosinase activity. Here, we show that in Streptomyces lividans TK64 harboring melC1 mutated and melC2 intact (melC1 - melC2 +) plasmids, while there was no tyrosinase activity, melC transcript was synthesized and apotyrosinase could be detected. The apotyrosinase could be activated to a limited degree by incubation with copper ions, or by mixing the mycelial extract from a culture harboring a melC1 - melC2 + (pPF950) plasmid with that from a culture containing a melC1 + melC2 - (pSA1) plasmid. Complementation analysis showed that melC1 acted in trans on the tyrosinase gene expression. Together, these results suggest that melC1 encodes or regulates a copper-transfer protein serving an in vivo copper-donor function in the biosynthesis of active tyrosinase.

Original languageEnglish
Pages (from-to)71-81
Number of pages11
Issue number1
StatePublished - 15 05 1988
Externally publishedYes


  • RNA analysis
  • Recombinant DNA
  • antibody affinity chromatography
  • apotyrosinase
  • complementation test
  • copper-transfer protein
  • gene expression
  • in vitro activation
  • melanin gene


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