The biochemical nature of the cell envelope of a high cellulase-secreting mutant differs from that of the Trichoderma reesei wild type

Nevalainen, Helena; Lavygina, Irina; Neethling, Diane; Packer, Nicolle H.

doi:10.1016/0168-1656(95)00064-w

Cited by 9 publications

(4 citation statements)

References 15 publications

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“…Carbohydrates are also present in cell wall glycoproteins and as space-filling interstitial components. Contrary to some earlier studies viewing the cell wall as a rather inert structure, in fact the fungal cell wall is a dynamic organelle, clearly shown in our studies comparing the composition of cell envelopes of the wild type and high-secreting Trichoderma reesei strains [5]. In addition to variation in the chitin and b-glucan content, a notable quantitative change was observed in the amount of cell envelope-associated protein upon induction of cellulase biosynthesis and secretion in a high cellulase-producing mutant strain.…”

Section: Introductioncontrasting

confidence: 99%

Proteins associated with the cell envelope of Trichoderma reesei : A proteomic approach

et al. 2001

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A total of 220 cell envelope-associated proteins were successfully extracted and separated from Trichoderma reesei mycelia actively synthesizing and secreting proteins and from mycelia in which the secretion of proteins are low. Altogether 56 spots were examined by nanoelectrospray tandem mass spectrometry and amino acid sequence was obtained for 32 spots. From these, 20 spots were identified by Advanced BLAST searches against all databases available to BLAST. The most abundant protein in both types of mycelia was HEX1, the major protein in Woronin body, a structure unique to filamentous fungi. Other proteins identified were vacuolar protease A, enolase, glyceraldehyde-3-phosphate dehydrogenase, transaldolase, protein disulfide isomerase, mitochondrial outer membrane porin, diphosphate kinase and translation elongation factor beta. Partial short amino acid sequence obtained from some proteins did not allow them to be assigned to a specific protein in the database by BLAST search. In some cases, the tandem mass spectrometry spectra were too complicated to be able to assign an amino acid sequence with certainty. The number of spots (12) giving a clear signal but finding no match in the databases suggests that a majority of proteins associated with a filamentous fungal cell wall, are novel. Some technical problems related to protein isolation are also discussed.

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Section: Introductioncontrasting

confidence: 99%

Proteins associated with the cell envelope of Trichoderma reesei : A proteomic approach

et al. 2001

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“…The fibrous material layer of QM9414 and PC-3-7 were 301.2 nm (±78.6) and 180.0 nm (±74.0), respectively, indicating a 40% reduction in thickness in PC-3-7 compared to QM9414. It has been reported that the cell wall of cellulase hyper-producing mutant contains less chitin than that of the wild-type strains and tends to be thinner (Nevalainen et al 1995). Our results are in agreement with this finding in that the cell envelope, including the fibrous material layer and the cell wall, of the hypercellulotic mutant PC-3-7 was thinner than that of QM9414 when cultured in Avicel-containing medium.…”

Section: Analysis Of the T Reesei Cell By Transmission Electron Microscopy (Tem)supporting

confidence: 92%

Ultrastructure of the cellulolytic fungus <i>Trichoderma reesei</i>

et al. 2015

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The cellulolytic fungus Trichoderma reesei is a potent cellulase producer and, therefore, cellulase hyper-producing mutants have been developed. However, morphological feature has still remained to be analyzed for understanding phenotypic change of T. reesei mutants. In this review, we show an electron microscopic observation of T. reesei to obtain new insights of morphological phenotypes of T. reesei mutants. We also successfully reconstructed the three dimensional structure of T. reesei hypha by using focused ion beam SEM technique.

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“…The traditional method of transformation of T. reesei is protoplast fusion (Penttilä et al, 1987). However, the technique has been particularly difficult with RUT-C30, seemingly due to a reduced ability of the strain to regenerate its cell wall (Nevalainen et al, 1995;Bergquist et al, 2002). Biolistic bombardment has provided a quick and reliable transformation system of T. reesei in general, whereby a good number of stable transformants are generated (Hazell et al, 2000;Te'o et al, 2002).…”

Section: Rut-c30 As a Host For Heterologous Protein Productionmentioning

confidence: 99%

Trichoderma reesei RUT-C30 – thirty years of strain improvement

2012

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The hypersecreting mutant Trichoderma reesei RUT-C30 (ATCC 56765) is one of the most widely used strains of filamentous fungi for the production of cellulolytic enzymes and recombinant proteins, and for academic research. The strain was obtained after three rounds of random mutagenesis of the wild-type QM6a in a screening program focused on high cellulase production and catabolite derepression. Whereas RUT-C30 achieves outstanding levels of protein secretion and high cellulolytic activity in comparison to the wild-type QM6a, recombinant protein production has been less successful. Here, we bring together and discuss the results from biochemical-, microscopic-, genomic-, transcriptomic-, glycomic-and proteomic-based research on the RUT-C30 strain published over the last 30 years.

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The biochemical nature of the cell envelope of a high cellulase-secreting mutant differs from that of the Trichoderma reesei wild type

Cited by 9 publications

References 15 publications

Proteins associated with the cell envelope of Trichoderma reesei : A proteomic approach

Proteins associated with the cell envelope of Trichoderma reesei : A proteomic approach

Ultrastructure of the cellulolytic fungus <i>Trichoderma reesei</i>

Trichoderma reesei RUT-C30 – thirty years of strain improvement

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