PMID:24498397

Citation	Michta, E, Ding, W, Zhu, S, Blin, K, Ruan, H, Wang, R, Wohlleben, W and Mast, Y (2014) Proteomic approach to reveal the regulatory function of aconitase AcnA in oxidative stress response in the antibiotic producer Streptomyces viridochromogenes Tü494. PLoS ONE 9:e87905
Abstract	The aconitase AcnA from the phosphinothricin tripeptide producing strain Streptomyces viridochromogenes Tü494 is a bifunctional protein: under iron-sufficiency conditions AcnA functions as an enzyme of the tricarboxylic acid cycle, whereas under iron depletion it is a regulator of iron metabolism and oxidative stress response. As a member of the family of iron regulatory proteins (IRP), AcnA binds to characteristic iron responsive element (IRE) binding motifs and post-transcriptionally controls the expression of respective target genes. A S. viridochromogenes aconitase mutant (MacnA) has previously been shown to be highly sensitive to oxidative stress. In the present paper, we performed a comparative proteomic approach with the S. viridochromogenes wild-type and the MacnA mutant strain under oxidative stress conditions to identify proteins that are under control of the AcnA-mediated regulation. We identified up to 90 differentially expressed proteins in both strains. In silico analysis of the corresponding gene sequences revealed the presence of IRE motifs on some of the respective target mRNAs. From this proteome study we have in vivo evidences for a direct AcnA-mediated regulation upon oxidative stress.
Links	PubMed PMC3912134 Online version:10.1371/journal.pone.0087905
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Annotations

Gene product	Qualifier	GO Term	Evidence Code	with/from	Aspect	Extension	Notes	Status
STRVR:Q9RIL1		GO:0010468: regulation of gene expression	ECO:0000315:		P		Refer to Table S1, "Proteins differentially expressed in S. viridochromogenes WT and MacnA due to oxidative stress treatment identified by MALDI TOF/TOF"	complete CACAO 9642

References

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