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  • 1
    Call number: 2020:98
    Keywords: Tier / Versuch
    Pages: 352 p. : ill.
    ISBN: 3-86025-195-3
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  • 2
    ISSN: 1432-0983
    Keywords: Trichoderma reesei ; Homologous transformation ; pyrG ; Vector integration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary The Trichoderma reesei orotidine-5′-phosphate decarboxylase gene was isolated by heterologous hybridization with the corresponding Neurospora gene as a probe. A 2.7 kb SalI fragment, which exclusively hybridized to the Neurospora gene, was subcloned in pGEM-5Zf(+). This subclone was termed pFG1 and was used to transform a Trichoderma reesei pyrG- negative mutant to PYR+. The transformation frequency in this homologous system was up to 12000 transformants per μg DNA. About one-fifth of the transformants tested were abortive. Perfect mitotic stability was found in half of the non-abortive transformants, correlating with vector integration at homologous and ectopic loci. In the unstable transformants the transforming DNA appears to be present in the form of extrachromosomal elements.
    Type of Medium: Electronic Resource
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  • 3
    ISSN: 1432-0983
    Keywords: Trichoderma reesei ; Cellobiohydrolase genes ; Cellulase formation ; Trichoderma sp
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Summary Eight different species of Trichoderma (T. virgatum, T. longibrachiatum, T. harzianum, T. pseudokoningii, T. polysporum, T. koningii, T. todica, T. saturnisporum), and three strains of T. reesei [QM 6a (wildtype), QM 9123 and QM 9414 (derived mutants)] were found to contain single copies of the cellobiohydrolase genes cbh1 and cbh2 in their genome. This was demonstrated by hybridization of the respective chromosomal DNAs with the corresponding gene fragments of T. reesei QM 9414. According to the relative position of cbh1 and cbh2 in Southern blots, T. harzianum, T. virgatum and T. saturnisporum were clearly distinguishable as unique species. Despite the presence of both cbh genes, these species did not form detectable cellobiohydrolase (CBH) I or II, or exhibit any cellulase activity. All other taxa were identical with respect to the genomic position of cbh1, formed two groups with respect to the position of cbh2, and produced varying amounts of CBH I and II. In all cases CBH I and II production correlated with the relative amount of cbh1- and cbh2-mRNA found. This was particularly true for the three strains of T. reesei, which secreted different amounts of CBH I and II, their efficiency to transcribe cbh1 and cbh2 having been increased as a result of mutation for higher cellulase production.
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  • 4
    ISSN: 1432-0983
    Keywords: DNA-protein interactions ; Trichoderma reseei ; cbh2 promoter ; β-glucuronidase
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract A 613-bp fragment of the 5′ upstream region of the Trichoderma reesei cbh2 gene (coding for the cellulolytic enzyme cellobiohydrolase II) has been isolated and sequenced. Fusion of this fragment to the E. coli uidA gene (coding for β-glucuronidase) leads to-albeit low-expression of β-glucuronidase activity in the presence of cellulose and upon the addition of low molecular weight inducers (sophorose, lactose) of cellobiohydrolase II. It also governed the formation of β-glucuronidase activity during sporulation and its transport to the conidial surface. However, despite the presence of a signal peptide in the cbh2:uidA fusion, β-glucuronidase was not secreted in T. reesei. Defined fragments of the 613-bp promoter region were isolated and used to identify areas involved in the regulation of cbh2 expression by protein-DNA binding assays. At least two binding areas-between-443/-363 and-363/-173, respectively-were identified. In both areas, the DNA-protein complex observed was appreciably larger when cell-free extracts from sophorose-induced mycelia were used. This suggests that at least one of the proteins regulating cbh2 transcription is itself induced by cellulose.
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  • 5
    ISSN: 1617-4623
    Keywords: Trichoderma reesei ; Aspergillus niger ; Protein kinase C gene ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract Oligonucleotides, designed on the basis of conserved flanking amino acid sequence segments within the catalytic domain of eukaryotic protein kinase C (PKC) proteins, were used as primers for polymerase chain reactions to amplify a 427-bp chromosomal DNA fragment from the filamentous fungusTrichoderma reesei. This fragment was then used to isolate genes encoding PKC homologues ofT. reesei andAspergillus niger (pkcl andpkcA, respectively). The genes contain six (T. reesei) and eight (A. niger) introns, which exhibit notable conservation in position with those found in the correspondingSchizosaccharomyces pombe pkc1 + andDrosophila melanogaster dPKC53Ebr genes. A single 4.2-kb transcript was detected in Northern analyses. The deduced PKC1 (T. reesei, 126 kDa) andPKCA (A. niger, 122 kDa) amino acid sequences reveal domains homologous to the Cl and C3/C4 domains of PKC-related proteins, but lack typical Ca2+-binding (C2) domains. Both contain a large, extended N-terminus, which shares a high degree of similarity with the corresponding regions ofSaccharomyces cerevisiae PKC1 andS. pombe pkc1+ and pkc2+ proteins, but which is not present in PKCs ofDictyostelium or higher eukaryotes. This extended region can be divided into three subdomains; the N-terminal one contains a hydrophobic helix-turn-helix motif, whereas the C-terminal one contains potential targets for proteolytic processing. A polyclonal antiserum raised against the pseudosubstrate-binding domain of PKC1 recognizes inT. reesei a 115–120 kDa protein in Western blots. Expression ofpkc1 cDNA in insect cells directs the synthesis of a PKC1 protein of similar size. TheT. reesei PKC1 protein was partially purified and some of its properties examined: it is stimulated about twofold by phospholipids or phorbol esters but is not stimulated by Ca2+. We conclude that these PKC proteins from filamentous fungi represent the Ca2+-insensitive fungal homologues of the nPKC family.
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  • 6
    ISSN: 1617-4623
    Keywords: Key words Trichoderma reesei ; Aspergillus niger ; Protein kinase C gene ; Signal transduction
    Source: Springer Online Journal Archives 1860-2000
    Topics: Biology
    Notes: Abstract  Oligonucleotides, designed on the basis of conserved flanking amino acid sequence segments within the catalytic domain of eukaryotic protein kinase C (PKC) proteins, were used as primers for polymerase chain reactions to amplify a 427-bp chromosomal DNA fragment from the filamentous fungus Trichoderma reesei. This fragment was then used to isolate genes encoding PKC homologues of T. reesei and Aspergillus niger (pkc1 and pkcA, respectively). The genes contain six (T. reesei) and eight (A. niger) introns, which exhibit notable conservation in position with those found in the corresponding Schizosaccharomyces pombe pkc1 + and Drosophila melanogaster dPKC53Ebr genes. A single 4.2-kb transcript was detected in Northern analyses. The deduced PKC1 (T. reesei, 126 kDa) and PKCA (A. niger, 122 kDa) amino acid sequences reveal domains homologous to the C1 and C3/C4 domains of PKC-related proteins, but lack typical Ca2+-binding (C2) domains. Both contain a large, extended N-terminus, which shares a high degree of similarity with the corresponding regions of Saccharomyces cerevisiae PKC1 and S. pombe pkc1+ and pkc2+ proteins, but which is not present in PKCs of Dictyostelium or higher eukaryotes. This extended region can be divided into three subdomains; the N-terminal one contains a hydrophobic helix-turn-helix motif, whereas the C-terminal one contains potential targets for proteolytic processing. A polyclonal antiserum raised against the pseudosubstrate-binding domain of PKC1 recognizes in T. reesei a 115–120 kDa protein in Western blots. Expression of pkc1 cDNA in insect cells directs the synthesis of a PKC1 protein of similar size. The T. reesei PKC1 protein was partially purified and some of its properties examined: it is stimulated about twofold by phospholipids or phorbol esters but is not stimulated by Ca2+. We conclude that these PKC proteins from filamentous fungi represent the Ca2+-insensitive fungal homologues of the nPKC family.
    Type of Medium: Electronic Resource
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