Journal of Microbiology and Biotechnology

  • 제16권6호
  • /
  • Pages.927-932
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  • 2006
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  • 1017-7825(pISSN)
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  • 1738-8872(eISSN)
한국미생물·생명공학회 (The Korean Society for Microbiology and Biotechnology)
권호 표지

S-Adenosylmethionine (SAM) Regulates Antibiotic Biosynthesis in Streptomyces spp. in a Mode Independent of Its Role as a Methyl Donor

  • Zhao Xin-Qing (Institute of Bioscience & Biotechnology and Department of Biological Science, Myong Ji University) ;
  • Jin Ying-Yu (Institute of Bioscience & Biotechnology and Department of Biological Science, Myong Ji University) ;
  • Kwon Hyung-Jin (Institute of Bioscience & Biotechnology and Department of Biological Science, Myong Ji University) ;
  • Yang Young-Yell (Institute of Bioscience & Biotechnology and Department of Biological Science, Myong Ji University) ;
  • Suh Joo-Won (Institute of Bioscience & Biotechnology and Department of Biological Science, Myong Ji University)
  • 발행 : 2006.06.01
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초록

S-Adenosylmethionine (SAM) is a ubiquitous biomolecule serving mainly as a methyl donor. Our recent studies revealed that SAM controls antibiotic production in Streptomyces. In this study, the functional mode of SAM was studied in S. coelicolor and S. antibioticus ATCC11891, employing S-adenosylhomocysteine (SAH), a methylation reaction product of SAM. Actinorhodin biosynthesis did not require SAM as a methyl donor, whereas SAH enhanced the actinorhodin biosynthesis up to the level comparable to SAM, and the most effective concentration of SAH was higher than that of SAM. In the case of oleandomycin that requires SAM for its biosynthesis, both SAM and SAH at the concentration as low as 100 mM showed comparable efficacy in enhancing the production; SAM at 1 mM concentration additionally stimulated to give a 5-fold enhancement of oleandomycin production. In vitro autophosphorylation of protein kinase AfsK was found to be activated by both SAM and SAH, as well as other structurally related compounds. Our studies demonstrate that SAM regulates antibiotic biosynthesis in a mode independent of its role as a methyl donor and suggest that SAM acts directly as an intracellular signaling molecule for Streptomyces.

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