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

Authors
Kim, Jin-SuLee, Han-NaLee, Heung-ShickKim, PilKim, Eung-Soo
Issue Date
Oct-2013
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
Streptomyces coelicolor; oxidative stress; wblA; spiA
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.23, no.10, pp.1365 - 1371
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
23
Number
10
Start Page
1365
End Page
1371
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/102101
DOI
10.4014/jmb.1306.06032
ISSN
1017-7825
Abstract
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 (stress protein interacting with WhcA) 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.
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