Comparative study of SoxR activation by redox‐active compounds. Issue 5 (17th October 2013)
- Record Type:
- Journal Article
- Title:
- Comparative study of SoxR activation by redox‐active compounds. Issue 5 (17th October 2013)
- Main Title:
- Comparative study of SoxR activation by redox‐active compounds
- Authors:
- Singh, Atul K.
Shin, Jung‐Ho
Lee, Kang‐Lok
Imlay, James A.
Roe, Jung‐Hye - Abstract:
- <abstract abstract-type="main"> <title>Summary</title> <p>SoxR from <italic>Escherichia coli</italic> and related enterobacteria is activated by a broad range of redox‐active compounds through oxidation or nitrosylation of its [2Fe–2S] cluster. Activated SoxR then induces SoxS, which subsequently activates more than 100 genes in response. In contrast, non‐enteric SoxRs directly activate their target genes in response to redox‐active compounds that include endogenously produced metabolites. We compared the responsiveness of SoxRs from <italic>Streptomyces coelicolor</italic> (ScSoxR), <italic>Pseudomonas aeruginosa</italic> (PaSoxR) and <italic>E. coli</italic> (EcSoxR), all expressed in <italic>S. coelicolor</italic>, towards natural or synthetic redox‐active compounds. EcSoxR responded to all compounds examined, whereas ScSoxR was insensitive to oxidants such as paraquat (Eh −440 mV) and menadione sodium bisulphite (Eh −45 mV) and to NO generators. PaSoxR was insensitive only to some NO generators. Whole‐cell EPR analysis of SoxRs expressed in <italic>E. coli</italic> revealed that the [2Fe–2S]<sup>1+</sup> of ScSoxR was not oxidizable by paraquat, differing from EcSoxR and PaSoxR. The mid‐point redox potential of purified ScSoxR was determined to be −185 ± 10 mV, higher by ∼ 100 mV than those of EcSoxR and PaSoxR, supporting its limited response to paraquat. The overall sensitivity profile indicates that both redox potential and kinetic reactivity determine the<abstract abstract-type="main"> <title>Summary</title> <p>SoxR from <italic>Escherichia coli</italic> and related enterobacteria is activated by a broad range of redox‐active compounds through oxidation or nitrosylation of its [2Fe–2S] cluster. Activated SoxR then induces SoxS, which subsequently activates more than 100 genes in response. In contrast, non‐enteric SoxRs directly activate their target genes in response to redox‐active compounds that include endogenously produced metabolites. We compared the responsiveness of SoxRs from <italic>Streptomyces coelicolor</italic> (ScSoxR), <italic>Pseudomonas aeruginosa</italic> (PaSoxR) and <italic>E. coli</italic> (EcSoxR), all expressed in <italic>S. coelicolor</italic>, towards natural or synthetic redox‐active compounds. EcSoxR responded to all compounds examined, whereas ScSoxR was insensitive to oxidants such as paraquat (Eh −440 mV) and menadione sodium bisulphite (Eh −45 mV) and to NO generators. PaSoxR was insensitive only to some NO generators. Whole‐cell EPR analysis of SoxRs expressed in <italic>E. coli</italic> revealed that the [2Fe–2S]<sup>1+</sup> of ScSoxR was not oxidizable by paraquat, differing from EcSoxR and PaSoxR. The mid‐point redox potential of purified ScSoxR was determined to be −185 ± 10 mV, higher by ∼ 100 mV than those of EcSoxR and PaSoxR, supporting its limited response to paraquat. The overall sensitivity profile indicates that both redox potential and kinetic reactivity determine the differential responses of SoxRs towards various oxidants.</p> </abstract> … (more)
- Is Part Of:
- Molecular microbiology. Volume 90:Issue 5(2013)
- Journal:
- Molecular microbiology
- Issue:
- Volume 90:Issue 5(2013)
- Issue Display:
- Volume 90, Issue 5 (2013)
- Year:
- 2013
- Volume:
- 90
- Issue:
- 5
- Issue Sort Value:
- 2013-0090-0005-0000
- Page Start:
- 983
- Page End:
- 996
- Publication Date:
- 2013-10-17
- Subjects:
- Molecular microbiology -- Periodicals
572.829 - Journal URLs:
- http://www.blackwell-synergy.com/servlet/useragent?func=showIssues&code=mmi&close=2003#C2003 ↗
http://onlinelibrary.wiley.com/journal/10.1111/(ISSN)1365-2958 ↗
http://onlinelibrary.wiley.com/ ↗ - DOI:
- 10.1111/mmi.12410 ↗
- Languages:
- English
- ISSNs:
- 0950-382X
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 5900.817960
British Library DSC - BLDSS-3PM
British Library STI - ELD Digital store - Ingest File:
- 3199.xml