The npgA/cfwA gene encodes a putative 4'-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans

Keszenman-Pereyra, David; Lawrence, Stephen J.; Twfieg, Mohammed-E.; Price, J.; Turner, Geoffrey

doi:10.1007/s00294-003-0382-7

Cited by 56 publications

(30 citation statements)

References 20 publications

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“…The high degree of amino acid conservation of FfPpt1 to Lys5p makes it very likely that FfPpt1 activates the F. fujikuroi α-aminoadipate reductase Aar1 in the same mode of action as Lys5p activates Lys2p. The involvement of FfPpt1 in lysine biosynthesis is consistent with the observations made in several filamentous ascomycetes [30], [33], [36]–[39], [41]. Since Ff ppt1 mutants were not viable without lysine supplementation it is suggested that FfAar1 cannot be post-translationally modified by the mitochondrial AcpS-type PPTase homolog.…”

Section: Discussionsupporting

confidence: 87%

“…Similarly to the findings in several filamentous ascomycetes [33]–[39], F. fujikuroi ppt1 mutants were not able to produce any PKS-derived products such as bikaverins, fusarubins or PKS/NRPS-derived fusarins. This is in agreement with the fact that Sfp-type PPTases are essential for 4′-phosphopantetheinylation of ACPs and PCPs in PKSs and NRPSs, respectively [25], [26].…”

Section: Discussionsupporting

confidence: 78%

“…The gene loci were designated npgA and cfwA , respectively [31], [32]. Later both loci were identified to be identical and encode a Sfp-type PPTase [33], [34] that is responsible for penicillin, siderophore (extracellular triacetyl fusarinine C and intracellular ferricrocin), emericellin, shamixanthone, dehydroaustinol, and lysine production [33]–[35]. Other examples for altered secondary metabolite spectra were found in npgA / ppt1 mutants of Colletotrichum graminicola [36], Penicillium chrysogenum [37], A. niger [38] and Trichoderma virens [39].…”

Section: Introductionmentioning

confidence: 99%

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The Sfp-Type 4′-Phosphopantetheinyl Transferase Ppt1 of Fusarium fujikuroi Controls Development, Secondary Metabolism and Pathogenicity

et al. 2012

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The heterothallic ascomycete Fusarium fujikuroi is a notorious rice pathogen causing super-elongation of plants due to the production of terpene-derived gibberellic acids (GAs) that function as natural plant hormones. Additionally, F. fujikuroi is able to produce a variety of polyketide- and non-ribosomal peptide-derived metabolites such as bikaverins, fusarubins and fusarins as well as metabolites from yet unidentified biosynthetic pathways, e.g. moniliformin. The key enzymes needed for their production belong to the family of polyketide synthases (PKSs) and non-ribosomal peptide synthases (NRPSs) that are generally known to be post-translationally modified by a Sfp-type 4′phosphopantetheinyl transferase (PPTase). In this study we provide evidence that the F. fujikuroi Sfp-type PPTase FfPpt1 is essentially involved in lysine biosynthesis and production of bikaverins, fusarubins and fusarins, but not moniliformin as shown by analytical methods. Concomitantly, targeted Ffppt1 deletion mutants reveal an enhancement of terpene-derived metabolites like GAs and volatile substances such as α-acorenol. Pathogenicity assays on rice roots using fluorescent labeled wild-type and Ffppt1 mutant strains indicate that lysine biosynthesis and iron acquisition but not PKS and NRPS metabolism is essential for establishment of primary infections of F. fujikuroi. Additionally, FfPpt1 is involved in conidiation and sexual mating recognition possibly by activating PKS- and/or NRPS-derived metabolites that could act as diffusible signals. Furthermore, the effect on iron acquisition of Ffppt1 mutants led us to identify a previously uncharacterized putative third reductive iron uptake system (FfFtr3/FfFet3) that is closely related to the FtrA/FetC system of A. fumigatus. Functional characterization provides evidence that both proteins are involved in iron acquisition and are liable to transcriptional repression of the homolog of the Aspergillus GATA-type transcription factor SreA under iron-replete conditions. Targeted deletion of the first Fusarium homolog of this GATA-type transcription factor-encoding gene, Ffsre1, strongly indicates its involvement in regulation of iron homeostasis and oxidative stress resistance.

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Section: Discussionsupporting

confidence: 87%

Section: Discussionsupporting

confidence: 78%

Section: Introductionmentioning

confidence: 99%

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The Sfp-Type 4′-Phosphopantetheinyl Transferase Ppt1 of Fusarium fujikuroi Controls Development, Secondary Metabolism and Pathogenicity

et al. 2012

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“…Cfw/NpgA, the Sfp-type PPTase from the fungus A. nidulans , is required for the production of several natural products, as well as conidiophore development, and was named for the phenotype of non-pigmented colonies. 67, 68 It was discovered that a single point mutation in this gene, L217R, resulted in a temperature sensitive strain of A. nidulans . 69 This residue is possibly required for protein stability, and mutation from a hydrophobic residue to a hydrophilic residue severely disrupts the solubility and stability of the PPTase NpgA.…”

Section: Structuresmentioning

confidence: 99%

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

et al. 2014

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Although holo-acyl carrier protein synthase, AcpS, a phosphopantetheinyl transferase (PPTase), was characterized in the 1960s, it was not until the publication of the landmark paper by Lambalot et al. in 1996 that PPTases garnered wide-spread attention being classified as a distinct enzyme superfamily. In the past two decades an increasing number of papers has been published on PPTases ranging from identification, characterization, structure determination, mutagenesis, inhibition, and engineering in synthetic biology. In this review, we comprehensively discuss all current knowledge on this class of enzymes that post-translationally install a 4′-phosphopantetheine arm on various carrier proteins.

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“…Recently, the npgA gene encoding a pantothenyl transferase was identified in the model filamentous fungus Aspergillus nidulans [9,10]. The npgA1 mutant displays null‐pigmentation (NPG) phenotypes and produces white conidia and hyphae throughout the whole life cycle [11,12].…”

Section: Introductionmentioning

confidence: 99%

ThesnpA, a temperature-sensitive suppressor ofnpgA1, encodes the eukaryotic translation release factor, eRF1, inAspergillus nidulans

Han

Kim

et al. 2005

FEMS Microbiology Letters

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The npgA1 mutation causes defects in the outer layer of the cell wall resulting in a colorless colony. In this study, a temperature-sensitive suppressor of npgA1 named snpA was isolated by UV mutagenesis. The suppressing mutant showed pleiotropic phenotypes in cellular structure and developmental processes when incubated at a temperature of 37 degrees C or above. At 37 degrees C, multiple germ tubes emerged from germinating conidia. Moreover, at 42 degrees C conidia germination was delayed more than 12h and hyphal growth was strongly inhibited. The suppressor allele, snpA6, is recessive and maps to the linkage group III. A gene complementing the mutation was identified employing the chromosome III-specific cosmid library. Sequencing analysis revealed that the snpA gene encodes the eukaryotic polypeptide release factor, eRF1. The snpA6 allele contains a G-A mutation resulting in SnpA(E117K), which may allow read-through of the nonsense mutation in the npgA1 allele in a similar manner to the yeast omni-potent suppressor SUP45 and SUP35.

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The npgA/cfwA gene encodes a putative 4'-phosphopantetheinyl transferase which is essential for penicillin biosynthesis in Aspergillus nidulans

Cited by 56 publications

References 20 publications

The Sfp-Type 4′-Phosphopantetheinyl Transferase Ppt1 of Fusarium fujikuroi Controls Development, Secondary Metabolism and Pathogenicity

The Sfp-Type 4′-Phosphopantetheinyl Transferase Ppt1 of Fusarium fujikuroi Controls Development, Secondary Metabolism and Pathogenicity

The phosphopantetheinyl transferases: catalysis of a post-translational modification crucial for life

ThesnpA, a temperature-sensitive suppressor ofnpgA1, encodes the eukaryotic translation release factor, eRF1, inAspergillus nidulans

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