Munnoch, JT and Martinez, MTP and Svistunenko, DA and Crack, JC and Le Brun, NE and Hutchings, MI (2016) Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily. Scientific Reports, 6 (1). 31597-. DOI https://doi.org/10.1038/srep31597
Munnoch, JT and Martinez, MTP and Svistunenko, DA and Crack, JC and Le Brun, NE and Hutchings, MI (2016) Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily. Scientific Reports, 6 (1). 31597-. DOI https://doi.org/10.1038/srep31597
Munnoch, JT and Martinez, MTP and Svistunenko, DA and Crack, JC and Le Brun, NE and Hutchings, MI (2016) Characterization of a putative NsrR homologue in Streptomyces venezuelae reveals a new member of the Rrf2 superfamily. Scientific Reports, 6 (1). 31597-. DOI https://doi.org/10.1038/srep31597
Abstract
Members of the Rrf2 superfamily of transcription factors are widespread in bacteria but their functions are largely unexplored. The few that have been characterized in detail sense nitric oxide (NsrR), iron limitation (RirA), cysteine availability (CymR) and the iron sulfur (Fe-S) cluster status of the cell (IscR). In this study we combined ChIP- and dRNA-seq with in vitro biochemistry to characterize a putative NsrR homologue in Streptomyces venezuelae. ChIP-seq analysis revealed that rather than regulating the nitrosative stress response like Streptomyces coelicolor NsrR, Sven6563 binds to a conserved motif at a different, much larger set of genes with a diverse range of functions, including a number of regulators, genes required for glutamine synthesis, NADH/NAD(P)H metabolism, as well as general DNA/RNA and amino acid/protein turn over. Our biochemical experiments further show that Sven6563 has a [2Fe-2S] cluster and that the switch between oxidized and reduced cluster controls its DNA binding activity in vitro. To our knowledge, both the sensing domain and the putative target genes are novel for an Rrf2 protein, suggesting Sven6563 represents a new member of the Rrf2 superfamily. Given the redox sensitivity of its Fe-S cluster we have tentatively named the protein RsrR for Redox sensitive response Regulator.
Item Type: | Article |
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Uncontrolled Keywords: | Streptomyces; Bacterial Proteins; Iron-Sulfur Proteins; Transcription Factors; DNA, Bacterial; Protein Binding; Sequence Homology, Amino Acid; Nucleotide Motifs |
Subjects: | Q Science > QH Natural history > QH426 Genetics |
Divisions: | Faculty of Science and Health Faculty of Science and Health > Life Sciences, School of |
SWORD Depositor: | Unnamed user with email elements@essex.ac.uk |
Depositing User: | Unnamed user with email elements@essex.ac.uk |
Date Deposited: | 17 Oct 2016 14:38 |
Last Modified: | 30 Oct 2024 20:22 |
URI: | http://repository.essex.ac.uk/id/eprint/17772 |
Available files
Filename: srep31597.pdf
Licence: Creative Commons: Attribution 3.0