Isolation and nature of intracellular alpha-aminoadipic acid-containing peptides from Paecilomyces persicinus P-10

Eriquez, L A; Pisano, Michael A.

doi:10.1128/aac.16.3.392

Cited by 17 publications

(4 citation statements)

References 22 publications

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“…in Acremonium and Cephaloporium genera as well (W. Gams, personal communications). The production of CPC in A. persicinum has shown to be 5 -8 mg/dl by Eriquez andMalowitz studies (Eriquez andPisano, 1979 andMalowitz, 1982), which was confirmed in this study to be 5 mg/dl (data not shown). Therefore, A. persicinum has not been applied for biotechnological processes due to its low CPC production.…”

Section: Discussionsupporting

confidence: 84%

Isolation of Acremonium species producing cephalosporine C (CPC) from forest soil in Gilan province, Iran

Sarookhani¹,

Moazzami²

2007

Afr. J. Biotechnol.

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Cephalosporin C (CPC) is a major precursor of cephalosporin antibiotics which is produced by a group of deuteromycets. After biosynthesis in optimized fermentation media, CPC is recovered and converted to a variety of potent cephalosporin antibiotic drugs. This study was performed to determine the mycoflora producing CPC in various parts of Iran soil. Soil samples were collected and cultured on selective media and Acremonium sp. were isolated. The presence of CPC antibiotic in the fermentation broths of these species was determined by a combination of biological, HPLC and mass spectrometry methods. From 350 fungi isolated, 21 (6%) were Acremonium spp, which one strain was able to produce CPC. This species was recognized as Acremonium persicinum according to its macroscopic and microscopic criteria. It is possible to apply different characteristics of the isolated species in strain optimization processes such as protoplast fusion.

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Section: Discussionsupporting

confidence: 84%

Isolation of Acremonium species producing cephalosporine C (CPC) from forest soil in Gilan province, Iran

Sarookhani¹,

Moazzami²

2007

Afr. J. Biotechnol.

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“…Cephalosporin C is a 13-lactam antibiotic formed in Cephalosporium acremonium (Acremonium chrysogenum; the name C. acremonium is used here to avoid confusion between Penicillium chrysogenum and A. chrysogenum) and other filamentous fungi by condensation of L-a-aminoadipic acid, L-cysteine, and L-valine (11,12). The first step in the cephalosporin-biosynthetic pathway involves a complex set of biochemical reactions ( Fig.…”

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confidence: 99%

Characterization of the Cephalosporium acremonium pcbAB gene encoding alpha-aminoadipyl-cysteinyl-valine synthetase, a large multidomain peptide synthetase: linkage to the pcbC gene as a cluster of early cephalosporin biosynthetic genes and evidence of multiple functional domains

et al. 1991

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A 24-kb region of Cephalosporium acremonium C10 DNA was cloned by hybridization with the pcbAB and pcbC genes of Penicillium chrysogenum. A 3.2-kb BamHI fragment of this region complemented the mutation in the structural pcbC gene of the C. acremonium N2 mutant, resulting in cephalosporin production. A functional alpha-aminoadipyl-cysteinyl-valine (ACV) synthetase was encoded by a 15.6-kb EcoRI-BamHI DNA fragment, as shown by complementation of an ACV synthetase-deficient mutant of P. chrysogenum. Two transcripts of 1.15 and 11.4 kb were found by Northern (RNA blot) hybridization with probes internal to the pcbC and pcbAB genes, respectively. An open reading frame of 11,136 bp was located upstream of the pcbC gene that matched the 11.4-kb transcript initiation and termination regions. It encoded a protein of 3,712 amino acids with a deduced Mr of 414,791. The nucleotide sequence of the gene showed 62.9% similarity to the pcbAB gene encoding the ACV synthetase of P. chrysogenum; 54.9% of the amino acids were identical in both ACV synthetases. Three highly repetitive regions occur in the deduced amino acid sequence of C. acremonium ACV synthetase. Each is similar to the three repetitive domains in the deduced sequence of P. chrysogenum ACV synthetase and also to the amino acid sequence of gramicidin synthetase I and tyrocidine synthetase I of Bacillus brevis. These regions probably correspond to amino acid activating domains in the ACV synthetase protein. In addition, a thioesterase domain was present in the ACV synthetases of both fungi. A similarity has been found between the domains existing in multienzyme nonribosomal peptide synthetases and polyketide and fatty acid synthetases. The pcbAB gene is linked to the pcbC gene, forming a cluster of early cephalosporin-biosynthetic genes.

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“…The presence of nonribosomal peptides in the culture of the penicillin or cephalosporin producers P. chrysogenum, Acremonium chrysogenum, and Paecilomyces persicinus (8,23) that are secreted into the culture broth (24) led us to study if these peptides or another secreted small molecule serves to induce penicillin biosynthesis.…”

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Characterization of an Autoinducer of Penicillin Biosynthesis in Penicillium chrysogenum

Martı́n

Garcı́a-Estrada

Rumbero

et al. 2011

Appl Environ Microbiol

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Filamentous fungi produce an impressive variety of secondary metabolites; many of them have important biological activities. The biosynthesis of these secondary metabolites is frequently induced by plant-derived external elicitors and appears to also be regulated by internal inducers, which may work in a way similar to that of bacterial autoinducers. The biosynthesis of penicillin in Penicillium chrysogenum is an excellent model for studying the molecular mechanisms of control of gene expression due to a good knowledge of the biochemistry and molecular genetics of ␤-lactam antibiotics and to the availability of its genome sequence and proteome. In this work, we first developed a plate bioassay that allows direct testing of inducers of penicillin biosynthesis using single colonies of P. chrysogenum. Using this bioassay, we have found an inducer substance in the conditioned culture broths of P. chrysogenum and Acremonium chrysogenum. No inducing effect was exerted by ␥-butyrolactones, jasmonic acid, or the penicillin precursor ␦-(L-␣-aminoadipyl)-L-cysteinyl-Dvaline. The conditioned broth induced penicillin biosynthesis and transcription of the pcbAB, pcbC, and penDE genes when added at inoculation time, but its effect was smaller if added at 12 h and it had no effect when added at 24 h, as shown by Northern analysis and lacZ reporter studies. The inducer molecule was purified and identified by mass spectrometry (MS) and nuclear magnetic resonance (NMR) as 1,3-diaminopropane. Addition of pure 1,3-diaminopropane stimulated the production of penicillin by about 100% compared to results for the control cultures. Genes for the biosynthesis of 1,3-diaminopropane have been identified in the P. chrysogenum genome.Filamentous fungi, particularly ascomycetes and basidiomycetes, are well-known producers of hundreds of bioactive secondary metabolites (40). The recent sequencing of the genomes of Aspergillus niger (28), Aspergillus nidulans (12, 50), Aspergillus oryzae (25), Penicillium chrysogenum (49), and the basidiomycete Pleurotus ostreatus (G. Pisabarro, personal communication) has provided evidence about the presence in their genomes of numerous gene clusters encoding nonribosomal peptide synthetases (NRPS), polyketide synthases (PKS), hybrid polyketide-nonribosomal peptide synthetases (HPS), isoprenoid synthetases, and other nonconventional antibiotic-synthesizing enzymes. Genome mining is a powerful tool for discovering new bioactive natural products (38).Penicillin biosynthesis in P. chrysogenum is an excellent model for understanding how those complex molecules are synthesized and how the cell controls their production, because its biochemistry and molecular genetics are very well known (26). Penicillin is produced by several filamentous fungi, of which P. chrysogenum (26), A. nidulans (4), and Penicillium nalgiovense (20) have been studied in more detail. The three enzymes ␣-aminoadipyl-cysteinyl-valine synthetase (ACVS), isopenicillin N synthase (IPNS), and isopenicillin N acyltransferase (IAT) are encoded, respe...

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Isolation and nature of intracellular alpha-aminoadipic acid-containing peptides from Paecilomyces persicinus P-10

Cited by 17 publications

References 22 publications

Isolation of Acremonium species producing cephalosporine C (CPC) from forest soil in Gilan province, Iran

Isolation of Acremonium species producing cephalosporine C (CPC) from forest soil in Gilan province, Iran

Characterization of the Cephalosporium acremonium pcbAB gene encoding alpha-aminoadipyl-cysteinyl-valine synthetase, a large multidomain peptide synthetase: linkage to the pcbC gene as a cluster of early cephalosporin biosynthetic genes and evidence of multiple functional domains

Characterization of an Autoinducer of Penicillin Biosynthesis in Penicillium chrysogenum

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