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A WblA-Binding Protein, SpiA, Involved in Streptomyces Oxidative Stress Response

  • Kim, Jin-Su (Department of Biological Engineering, Inha University) ;
  • Lee, Han-Na (Department of Biological Engineering, Inha University) ;
  • Lee, Heung-Shick (Department of Biotechnology and Bioinformatics, Korea University) ;
  • Kim, Pil (Division of Biotechnology, The Catholic University of Korea) ;
  • Kim, Eung-Soo (Department of Biological Engineering, Inha University)
  • 투고 : 2013.06.13
  • 심사 : 2013.07.16
  • 발행 : 2013.10.28

초록

The Streptomyces coelicolor wblA gene is known to play a negative role in both antibiotic biosynthesis and the expression of genes responding to oxidative stress. Recently, WhcA, a WblA ortholog protein, was confirmed to interact with dioxygenase-encoding SpiA ($\underline{s}$tress $\underline{p}$rotein $\underline{i}$nteracting with Whc$\underline{A}$) in Corynebacterium glutamicum. We describe here the identification of a SpiA ortholog SCO2553 protein ($SpiA_{sc}$) that interacts with WblA in S. coelicolor. Using heterologous expression in E. coli and in vitro pull-down assays, we show that WblA specifically binds $SpiA_{sc}$, and is influenced by oxidants such as diamide. These data indicate that the interaction between WblA and $SpiA_{sc}$ is not only specific but also modulated by the redox status of the cell. Moreover, a $spiA_{sc}$-disruption mutant exhibited a less sensitive response to the oxidative stress induced by diamide present in solid plate culture. Real-time RT-PCR analysis also showed that transcription levels of oxidative stress response genes (sodF, sodF2, and trxB) were higher in the $spiA_{sc}$-deletion mutant than in wild-type S. coelicolor. These results show that $SpiA_{sc}$ negatively regulates WblA during oxidative stress responses in S. coelicolor.

키워드

참고문헌

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