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σ E ‐dependent activation of RbpA controls transcription of the furA‐katG operon in response to oxidative stress in mycobacteria
Author(s) -
Hu Yangbo,
Wang Zhongwei,
Feng Lipeng,
Chen Zhenkang,
Mao Chunyou,
Zhu Yan,
Chen Shiyun
Publication year - 2016
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13449
Subject(s) - operon , mycobacterium smegmatis , biology , transcription (linguistics) , oxidative stress , transcription factor , sigma factor , oxidative phosphorylation , microbiology and biotechnology , transcriptional regulation , mutant , regulation of gene expression , gene , promoter , gene expression , mycobacterium tuberculosis , biochemistry , tuberculosis , medicine , linguistics , philosophy , pathology
Summary Mycobacterium tuberculosis adopts various strategies to cope with oxidative stress during infection. Transcriptional regulators, including σ factors, make important contributions to this stress response, but how these proteins cooperate with each other is largely unknown. In this study, the role of RbpA and its cooperation with σ factors in response to oxidative stress are investigated. Knock down expression of rbpA in Mycobacterium smegmatis attenuated bacterial survival in the presence of H 2 O 2 . Additionally, transcription of the rbpA gene was induced by H 2 O 2 in a σ E ‐dependent manner. After induction, RbpA interacts with the principal sigma factor, σ A , to control the transcription of furA‐katG operon, which encodes an H 2 O 2 scavenging enzyme. Moreover, this regulation is responsible for the role of σ E in oxidative response because bacterial survival was attenuated and transcription of the furA‐katG operon was down‐regulated with H 2 O 2 treatment in sigE deletion mutant ( Δ sigE ), and over‐expression of RbpA in Δ sigE strain restored all of these phenotypes. Taken together, our study first illustrated a mechanism for σ E in response to oxidative stress through regulation of rbpA transcription. This study was also the first to demonstrate that RbpA is required for the full response to oxidative stress by cooperating with the principal σ A .