Phosphinothricin-tripeptide biosynthesis: An original version of bacterial secondary metabolism?

Schinko, Eva; Schad, Klaus; Eys, Sema; Keller, Ullrich; Wohlleben, Wolfgang

doi:10.1016/j.phytochem.2009.09.002

Cited by 20 publications

(22 citation statements)

References 102 publications

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“…This herbicidal and antibiotic compound produced by some Streptomyces strains [62], presents two alanines and the glutamate toxic analogue phosphinotricine. Strain 20PS01 showed an increased sensitivity to Bialaphos (Figure 3); a concentration of 100 µg/ml inhibited the growth of the hfq mutant, whereas a concentration 2.5-fold higher was required to obtain the same degree of growth inhibition in the wild type strain (Figure 3).…”

Section: Resultsmentioning

confidence: 99%

Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011

Sobrero

Schlüter

Lanner³

et al. 2012

PLoS ONE

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Riboregulation stands for RNA-based control of gene expression. In bacteria, small non-coding RNAs (sRNAs) are a major class of riboregulatory elements, most of which act at the post-transcriptional level by base-pairing target mRNA genes. The RNA chaperone Hfq facilitates antisense interactions between target mRNAs and regulatory sRNAs, thus influencing mRNA stability and/or translation rate. In the α-proteobacterium Sinorhizobium meliloti strain 2011, the identification and detection of multiple sRNAs genes and the broadly pleitropic phenotype associated to the absence of a functional Hfq protein both support the existence of riboregulatory circuits controlling gene expression to ensure the fitness of this bacterium in both free living and symbiotic conditions. In order to identify target mRNAs subject to Hfq-dependent riboregulation, we have compared the proteome of an hfq mutant and the wild type S. meliloti by quantitative proteomics following protein labelling with 15N. Among 2139 univocally identified proteins, a total of 195 proteins showed a differential abundance between the Hfq mutant and the wild type strain; 65 proteins accumulated ≥2-fold whereas 130 were downregulated (≤0.5-fold) in the absence of Hfq. This profound proteomic impact implies a major role for Hfq on regulation of diverse physiological processes in S. meliloti, from transport of small molecules to homeostasis of iron and nitrogen. Changes in the cellular levels of proteins involved in transport of nucleotides, peptides and amino acids, and in iron homeostasis, were confirmed with phenotypic assays. These results represent the first quantitative proteomic analysis in S. meliloti. The comparative analysis of the hfq mutant proteome allowed identification of novel strongly Hfq-regulated genes in S. meliloti.

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Section: Resultsmentioning

confidence: 99%

Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011

Sobrero

Schlüter

Lanner³

et al. 2012

PLoS ONE

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“…Streptomyces viridochromogenes Tü494 is the producer of the herbicide antibiotic phosphinothricin tripeptide (PTT). In this strain the function of the protein AcnA was analyzed in detail previously, because it represents a nodal point between primary and secondary metabolism [2]–[4]. It has been shown before that an S. viridochromogenes aconitase mutant (MacnA) is unable to form any aerial mycelium, spores nor PTT [3].…”

Section: Introductionmentioning

confidence: 99%

Proteomic Approach to Reveal the Regulatory Function of Aconitase AcnA in Oxidative Stress Response in the Antibiotic Producer Streptomyces viridochromogenes Tü494

Michta

Ding²,

Zhu³

et al. 2014

PLoS ONE

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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.

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“…It encodes a protein of 943 amino acid residues with a calculated molecular mass of 102,168 Da (Schaffer et al, 2001). It shows 59% sequence identity to AcnA of Escherichia coli and 47% sequence identity to human IRP1 (iron regulatory protein 1) and thus belongs to family II within the aconitase superfamily (Gruer et al, 1997a;Makarova and Koonin, 2003;Schinko et al, 2009). The three cysteine residues which coordinate the [4Fe-4S] cluster are located at positions 479, 545 and 548.…”

Section: Introductionmentioning

confidence: 99%

Biochemical characterisation of aconitase from Corynebacterium glutamicum

Baumgart

Bott

2011

Journal of Biotechnology

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Phosphinothricin-tripeptide biosynthesis: An original version of bacterial secondary metabolism?

Cited by 20 publications

References 102 publications

Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011

Quantitative Proteomic Analysis of the Hfq-Regulon in Sinorhizobium meliloti 2011

Proteomic Approach to Reveal the Regulatory Function of Aconitase AcnA in Oxidative Stress Response in the Antibiotic Producer Streptomyces viridochromogenes Tü494

Biochemical characterisation of aconitase from Corynebacterium glutamicum

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