Genomic organization of a polygalacturonase gene from a hyperpectinolytic mutant strain of Penicillium occitanis

Trigui-Lahiani, Héla; Ayadi, Malika; Hadj-Taieb, Noomen; Ali, Mamdouh Ben; Gargouri, Ali

doi:10.1111/j.1574-6968.2008.01071.x

Cited by 11 publications

(4 citation statements)

References 25 publications

(35 reference statements)

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“…The boundary junctions (GTA...YAG) and the putative Lariat branch point sequence (RCTRAY) are almost similar to those found in other fungal genes [28,29] (Table 2). …”

Section: Resultsmentioning

confidence: 73%

Cloning and Genomic Organization of a Rhamnogalacturonase Gene from Locally Isolated Strain of Aspergillus niger

Damak

Abdeljalil

Taeib

et al. 2015

Appl Biochem Biotechnol

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The rhg gene encoding a rhamnogalacturonase was isolated from the novel strain A1 of Aspergillus niger. It consists of an ORF of 1.505 kb encoding a putative protein of 446 amino acids with a predicted molecular mass of 47 kDa, belonging to the family 28 of glycosyl hydrolases. The nature and position of amino acids comprising the active site as well as the three-dimensional structure were well conserved between the A. niger CTM10548 and fungal rhamnogalacturonases. The coding region of the rhg gene is interrupted by three short introns of 56 (introns 1 and 3) and 52 (intron 2) bp in length. The comparison of the peptide sequence with A. niger rhg sequences revealed that the A1 rhg should be an endo-rhamnogalacturonases, more homologous to rhg A than rhg B A. niger known enzymes. The comparison of rhg nucleotide sequence from A. niger A1 with rhg A from A. niger shows several base changes. Most of these changes (59 %) are located at the third base of codons suggesting maintaining the same enzyme function. We used the rhamnogalacturonase A from Aspergillus aculeatus as a template to build a structural model of rhg A1 that adopted a right-handed parallel β-helix.

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“…The boundary junctions (GTA...YAG) and the putative Lariat branch point sequence (RCTRAY) are almost similar to those found in other fungal genes [28,29] (Table 2). …”

Section: Resultsmentioning

confidence: 73%

Cloning and Genomic Organization of a Rhamnogalacturonase Gene from Locally Isolated Strain of Aspergillus niger

Damak

Abdeljalil

Taeib

et al. 2015

Appl Biochem Biotechnol

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“…Three clones (72, 94 and 64) showed overlapping sequences for a pectin lyase (pnl) which allowed us to reconstruct a full length cDNA of pnl1 of P. occitanis (Trigui-Lahiani and Gargouri 2007). Two clones (8 and 3) derived from the same polygalacturonase (pga1) gene (Trigui-Lahiani et al 2008) and finally three clones (31, 1 and 12) correspond to the same pectate lyase (pal1) gene. As shown in Fig.…”

Section: Isolation Of Pectinase Cdna Probesmentioning

confidence: 99%

Constitutive over-expression of pectinases in Penicillium occitanis CT1 mutant is transcriptionally regulated

et al. 2011

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The CT1 mutant of Penicillium occitanis hyperproduces extracellular pectinases constitutively since it secretes pectinases even on glucose-containing medium. We show here that all other hydrolytic enzymes remain at low activities in CT1, confirming the specificity of the regulatory mutation towards pectinases. We isolated, by RT-PCR and through the construction of a cDNA library, three fragments coding for: a pectin lyase (pnl1), a polygalacturonase (pga1) and a pectate lyase (pal1). These fragments were used as probes in Northern blots analysis of the wild type strain CL100 and the CT1 mutant of P. occitanis grown in three culture conditions. The CT1 mutant showed a very high amount of pnl1, pga1 and pal1 mRNA either in pectin, glucose or glycerol grown cells while in the wild type CL100 strain, all transcripts were undetectable even on pectin. These results suggest that the CT1 mutation affects a trans-regulatory transcriptional factor regulating pectinase expression.

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“…A mutant exhibiting constitutive and specific overproduction of pectinases was previously isolated by classical nitrous acid mutagenesis. The mutant secretes large amounts of different pectinolytic enzymes both when grown under inducing (pectin) or repressing conditions (glucose) (Trigui-Lahiani et al, 2008 ). The nature of the mutation(s) causing the pectinolytic overproduction phenotype is unknown.…”

Section: Introductionmentioning

confidence: 99%

Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen Fusarium oxysporum

et al. 2017

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Penicillium occitanis is a model system for enzymatic regulation. A mutant strain exhibiting constitutive overproduction of different pectinolytic enzymes both under inducing (pectin) or repressing conditions (glucose) was previously isolated after chemical mutagenesis. In order to identify the molecular basis of this regulatory mechanism, the genomes of the wild type and the derived mutant strain were sequenced and compared, providing the first reference genome for this species. We used a phylogenomic approach to compare P. occitanis with other pectinolytic fungi and to trace expansions of gene families involved in carbohydrate degradation. Genome comparison between wild type and mutant identified seven mutations associated with predicted proteins. The most likely candidate was a mutation in a highly conserved serine residue of a conserved fungal protein containing a GAL4-like Zn2Cys6 binuclear cluster DNA-binding domain and a fungus-specific transcription factor regulatory middle homology region. To functionally characterize the role of this candidate gene, the mutation was recapitulated in the predicted orthologue Fusarium oxysporum, a vascular wilt pathogen which secretes a wide array of plant cell wall degrading enzymes, including polygalacturonases, pectate lyases, xylanases and proteases, all of which contribute to infection. However, neither the null mutant nor a mutant carrying the analogous point mutation exhibited a deregulation of pectinolytic enzymes. The availability, annotation and phylogenomic analysis of the P. occitanis genome sequence represents an important resource for understanding the evolution and biology of this species, and sets the basis for the discovery of new genes of biotechnological interest for the degradation of complex polysaccharides.

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Genomic organization of a polygalacturonase gene from a hyperpectinolytic mutant strain of Penicillium occitanis

Cited by 11 publications

References 25 publications

Cloning and Genomic Organization of a Rhamnogalacturonase Gene from Locally Isolated Strain of Aspergillus niger

Cloning and Genomic Organization of a Rhamnogalacturonase Gene from Locally Isolated Strain of Aspergillus niger

Constitutive over-expression of pectinases in Penicillium occitanis CT1 mutant is transcriptionally regulated

Regulatory Mechanisms of a Highly Pectinolytic Mutant of Penicillium occitanis and Functional Analysis of a Candidate Gene in the Plant Pathogen Fusarium oxysporum

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