S-Adenosyl-L-methionine Activates Actinorhodin Biosynthesis by Increasing Autophosphorylation of the Ser/Thr Protein Kinase AfsK in Streptomyces coelicolor A3(2)
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- JIN Ying-Yu
- Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University
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- CHENG Jinhua
- Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University
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- YANG Seung Hwan
- Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University
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- MENG Lingzhu
- Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University
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- PALANIYANDI Sasikumar Arunachalam
- Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University
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- ZHAO Xin-Qing
- Department of Bioscience and Bioengineering, Dalian University of Technology
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- SUH Joo-Won
- Division of Bioscience and Bioinformatics, College of Natural Science, Myongji University
Bibliographic Information
- Other Title
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- <i>S</i>-Adenosyl-<scp>L</scp>-methionine Activates Actinorhodin Biosynthesis by Increasing Autophosphorylation of the Ser/Thr Protein Kinase AfsK in<i>Streptomyces coelicolor</i>A3(2)
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Abstract
S-Adenosyl-L-methionine (SAM) is one of the major methyl donors in all living organisms. The exogenous treatment with SAM leads to increased actinorhodin production in Streptomyces coelicolor A3(2). In this study, mutants from different stages of the AfsK-AfsR signal transduction cascade were used to test the possible target of SAM. SAM had no significant effect on actinorhodin production in afsK, afsR, afsS, or actII-open reading frame 4 (ORF4) mutant. This confirms that afsK plays a critical role in delivering the signal generated by exogenous SAM. The afsK-pHJL-KN mutant did not respond to SAM, suggesting the involvement of the C-terminal of AfsK in binding with SAM. SAM increased the in vitro autophosphorylation of kinase AfsK in a dose-dependent manner, and also abolished the effect of decreased actinorhodin production by a Ser/Thr kinase inhibitor, K252a. In sum, our results suggest that SAM activates actinorhodin biosynthesis in S. coelicolor M130 by increasing the phosphorylation of protein kinase AfsK.
Journal
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- Bioscience, Biotechnology, and Biochemistry
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Bioscience, Biotechnology, and Biochemistry 75 (5), 910-913, 2011
Japan Society for Bioscience, Biotechnology, and Agrochemistry
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Keywords
Details 詳細情報について
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- CRID
- 1390282681455227264
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- NII Article ID
- 10028272608
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- NII Book ID
- AA10824164
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- ISSN
- 13476947
- 09168451
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- NDL BIB ID
- 11088665
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed