Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans

Punt, Peter J.; Dingemanse, Maria A.; Jacobs-Meijsing, Brigit J.M.; Pouwels, Peter H.; Hondel, Cees A. M. J. J. van den

doi:10.1016/0378-1119(88)90377-0

Cited by 151 publications

(85 citation statements)

References 47 publications

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“…The 1782 bp NcoI-SalI fragment was cloned between the 2-3 kb KpnI-NcoI fragment of the gpdA (glyceraldehyde-3-phosphate dehydrogenase) promoter from A . nidulans (Punt et al, 1988(Punt et al, ,1990) and the 710 bp BamHI-X6aI fragment of the trpC terminator (Mullaney et al, 1985) in pUC19. Similarly, the 1956 bp NcoI-EcoRI fragment of the A .…”

Section: Construction Of 1 Libraries and Isolation Of Phytase Genesmentioning

confidence: 99%

The Phytase Subfamily of Histidine Acid Phosphatases: Isolation of Genes for Two Novel Phytases from the Fungi Aspergillus Terreus and Myceliophthora Thermophila

Mitchell¹,

et al. 1997

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Phytases catalyse the hydrolysis of phytate (myo-inositol hexakisphosphate) to myo-inositol and inorganic phosphate. In this study genes encoding novel phytases from two different filamentous fungi, Aspergillus terreus strain 9A-1 and Myceliophthora thermophila were isolated. The encoded PhyA phytase proteins show 60% (A. terreus) and 489'0 (M. thermophila) identity, respectively, to the PhyA of Aspergillus niger and have 21-29% identity compared to other histidine acid phosphatases. All three PhyA proteins, in contrast to the A. niger pH 25-optimum acid phosphatase, prefer phytic acid as substrate and show enzyme activity at a broad range of acidic pH values. Based on their enzyme characteristics and protein sequence homology, the phytases form a novel subclass of the histidine acid phosphatase family.

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Section: Construction Of 1 Libraries and Isolation Of Phytase Genesmentioning

confidence: 99%

The Phytase Subfamily of Histidine Acid Phosphatases: Isolation of Genes for Two Novel Phytases from the Fungi Aspergillus Terreus and Myceliophthora Thermophila

Mitchell¹,

et al. 1997

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“…In all Podospora vectors, expression of the HET-s constructs was driven by the GPD promoter of Aspergillus nidulans (Punt et al, 1988). For construction of the pGPD-het-s(157-289) plasmid, the region encoding the C-terminal part of HET-s (residue 157 to 289) was amplified using the polymerase chain reaction (PCR) (oligonucleotides 5′-ATCCATGGAGAAAATAGTCGA-3′ and 5′-TAA-GATCTTTTAGTGATGATGGTGATGGTG-3′) and cloned as a NcoIBglII fragment into the NcoI and BamHI sites of the pAN52.1 vector (Punt et al, 1988).…”

Section: Plasmidsmentioning

confidence: 99%

“…For construction of the pGPD-het-s(157-289) plasmid, the region encoding the C-terminal part of HET-s (residue 157 to 289) was amplified using the polymerase chain reaction (PCR) (oligonucleotides 5′-ATCCATGGAGAAAATAGTCGA-3′ and 5′-TAA-GATCTTTTAGTGATGATGGTGATGGTG-3′) and cloned as a NcoIBglII fragment into the NcoI and BamHI sites of the pAN52.1 vector (Punt et al, 1988). For construction of the pGPD-het-S(157-289) plasmid, the pGPD-het-S vector (Coustou-Linares et al, 2001) was amplified by inverse PCR (oligonucleotides Nco157 5′-CATGC-CATGGGCGAGAAAATAGTCGACCAGG-3′ and NcoGPD 5′-CAT-GCCATGGTGATGTCTGCTCAAGC-3′).…”

Section: Plasmidsmentioning

confidence: 99%

“…For construction of the pGPD-het-S(157-289) plasmid, the pGPD-het-S vector (Coustou-Linares et al, 2001) was amplified by inverse PCR (oligonucleotides Nco157 5′-CATGC-CATGGGCGAGAAAATAGTCGACCAGG-3′ and NcoGPD 5′-CAT-GCCATGGTGATGTCTGCTCAAGC-3′). The PCR product was digested by NcoI and cloned into the NcoI site of the pAN52.1 vector (Punt et al, 1988). For construction of the pGPD-het-s(157-289)-GFP plasmid, the 5′ region of the het-s ORF allowing expression of peptide was amplified by PCR (oligonucleotides: 5′-CC-CTCATGATGGAGAAAATAGTCGACCAGGTC-3′ and 5′-CCCT-CATGACATTATCCCAGAACCCCTTAC-3′).…”

Section: Plasmidsmentioning

confidence: 99%

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The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo

Balguerie

Reis

Coulary‐Salin

et al. 2004

Journal of Cell Science

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The [Het-s] prion of the fungus Podospora anserina propagates as a self-perpetuating amyloid form of the HET-s protein. This protein triggers a cell death reaction termed heterokaryon incompatibility when interacting with the HET-S protein, an allelic variant of HET-s. HET-s displays two distinct domains, a N-terminal globular domain and a C-terminal unstructured prion-forming domain (residues 218-289). Here, we describe the characterization of HET-s(157-289), a truncated form of HET-s bearing an extensive deletion in the globular domain but retaining full activity in incompatibility and prion propagation. In vitro, HET-s(157-289) polymerizes into amyloid fibers displaying the same core region as full-length HET-s fibers. We have shown previously that fusions of green fluorescent protein (GFP) with HET-s or HET-s(218-289) form dot-like aggregates in vivo upon transition to the prion state. By contrast, a HET-s(157-289)/GFP fusion protein forms elongated fibrillar aggregates in vivo. Such elongated aggregates can reach up to 150 μm in length. The in vivo dynamics of these organized structures is analysed by time lapse microscopy. We find that the large elongate structures grow by lateral association of shorter fibrillar aggregates. When co-expressed with HET-s(157-289), full-length HET-s and HET-s(218-289) can be incorporated into such elongated aggregates. Together, our data indicate that HET-s(157-289) aggregates can adopt an organized higher-order structure in vivo and that the ability to adopt this supramolecular organization is conferred by the sequences appended to the amyloid core region.

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“…It did not increase in intensity upon hybridization at lower stringency so it seems unlikely that this band indicates another gpd copy, though this cannot be completely excluded. The additional HindIII sites might be located just outside the available cDNA sequence, or in introns; the gpd gene of A. nidulans contains seven introns, five in or before the translational start site, and two near the 3' end (Punt et al, 1988).…”

Section: Characterization Of Gpd Sequencesmentioning

confidence: 99%

Glyceraldehyde-3-phosphate dehydrogenase expression in Trichoderma harzianum is repressed during conidiation and mycoparasitism

Puyesky

Ponce-Noyola²,

Horwitz³

et al. 1997

Microbiology

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A glyceraldehyde-3-phosphate dehydrogenase (gpd) cDNA was isolated from the filamentous fungus Trichalenna hanianum in the course of a search for light-regulated genes in this organism. There is apparently only one copy of gpd in the T. hamianurn genome, and its sequence is most similar to that of other filamentous ascomycetes. Trichoderme grows in the soil as a saprophyte or mycoparasite. A brief pulse of blue light, or nutrient depletion, induces sporulation, which is accompanied by altered patterns of abundance of specific

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Isolation and characterization of the glyceraldehyde-3-phosphate dehydrogenase gene of Aspergillus nidulans

Cited by 151 publications

References 47 publications

The Phytase Subfamily of Histidine Acid Phosphatases: Isolation of Genes for Two Novel Phytases from the Fungi Aspergillus Terreus and Myceliophthora Thermophila

The Phytase Subfamily of Histidine Acid Phosphatases: Isolation of Genes for Two Novel Phytases from the Fungi Aspergillus Terreus and Myceliophthora Thermophila

The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo

Glyceraldehyde-3-phosphate dehydrogenase expression in Trichoderma harzianum is repressed during conidiation and mycoparasitism

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