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1

Heterologous expression of genes in filamentous fungi

100%
Kruszewska J. S.
Acta Biochimica Polonica
|
1999
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tom 46
|
nr 1
Isolation of some biologically important proteins from natural sources was found to be too expensive or scarcely possible (human proteins). The problem could be solved by expression of heterologous genes. Many biologically active proteins have been successfully expressed in filamentous fungi, some of them, however, at a low level. Thus, improvement of this technique appears to be a very important task. The process comprises several steps. Some of them, such as efficient transformation, vector construction, processing of signal sequences, post-translational modifications and secretion of the expressed proteins, have been intensively investigated. This review presents obstacles and problems encountered in expression of heterologous genes and discusses strategies of development in this area.
2

Solubilization and one-step purification of mannosylphosphodolichol synthase from Trichoderma reesei

51%
Kruszewska J. S., Perlinska-Lenart U., Palamarczyk G.
Acta Biochimica Polonica
|
1996
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tom 43
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nr 2
Mannosylphosphodolichol synthase (MPD-synthase) (EC 2.4.1.830) catalyzing formation of MPD from GDPMan and dolichylphosphate (PD) has been purified from T. reesei cellular membranes almost to homogeneity. Selective solubilization of the enzyme was followed by one step purification on Phenyl-Sepharose column. SDS/ PAGE of the purified enzyme fraction revealed the presence of a protein band of 31 kDa corresponding to the apparent molecular mass of the MPD-synthase purified from S. cerevisiae [Babczinski, P. et al. (1980) Eur. J. Biochem. 105,509-515; Haselbeck A. (1989) Eur. /. Biochem. 181, 663-6681. During solubilization, the enzyme was stabilized by the presence of a lipophilic substrate dolichylphosphate and phospholipids as well as by protease inhibitors. The Phenyl-Sepharose purified enzyme had an absolute requirement for dolichylphosphate and was activated by cAMP dependent protein kinase.
3

Disruption of Trichoderma reesei gene encoding protein O-mannosyl-transferase I results in a decrease of the enzyme activity and alteration of cell wall composition

39%
Gorka-Niec W., Pniewski M., Kania A., Perlinska-Lenart U., Palamarczyk G., Kruszewska J. S.
Acta Biochimica Polonica
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2008
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tom 55
|
nr 2
251-259
In fungi transfer of the first mannosyl residue to proteins during their O-glycosylation is catalyzed by protein O-mannosyltransferases encoded by pmt genes. Disruption of the pmt1gene in Trichodermacaused a significant decrease in the total activity of protein O-mannosyltransferases. Moreover, disruption of the pmt1gene also led to osmotic sensitivity of the strain, indicating an essential role of the PMTI protein activity for cell wall synthesis. At the same time, the strain was defective in septa formation, producing only half the number of septa per unit length of hypha compared with the wild type. Disruption of the pmt1gene decreased protein secretion but had no effect on glycosylation of secreted proteins, which suggests that PMTI protein O-mannosyltranferase does not take part in glycosylation of these proteins.
4

Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi

39%
Kruszewska J. S., Perlinska-Lenart U., Gorka-Niec W., Orlowski J., Zembek P., Palamarczyk G.
Acta Biochimica Polonica
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2008
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tom 55
|
nr 3
447-456
Due to its natural properties, Trichoderma reesei is commonly used in industry-scale production of secretory proteins. Since almost all secreted proteins are O-glycosylated, modulation of the activity of enzymes of the O-glycosylation pathway are likely to affect protein production and secretion or change the glycosylation pattern of the secreted proteins, altering their stability and biological activity. Understanding how the activation of different components of the O-glycosylation pathway influences the glycosylation pattern of proteins and their production and secretion could help in elucidating the mechanism of the regulation of these processes and should facilitate creation of engineered microorganisms producing high amounts of useful proteins. In this review we focus on data concerning Trichoderma, but also present some background information allowing comparison with other fungal species.
5

Molecular characterization of central cytoplasmic loop in Aspergillus nidulans AstA transporter

39%
Pilsyk S., Sienko M., Brzywczy J., Golan M. P., Perlinska-Lenart U., Kruszewska J. S.
Acta Biochimica Polonica
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2018
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tom 65
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nr 4
6

Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation

39%
Perlinska-Lenart U., Kurzatkowski W., Janas P., Kopinska A., Palamarczyk G., Kruszewska J. S.
Acta Biochimica Polonica
|
2005
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tom 52
|
nr 1
O-glycosylation has been considered a limiting factor in protein secretion in filamentous fungi. Overexpression of the yeast DPM1 gene encoding dolichylphosphate mannose synthase (DPMS) in an Aspergillus nidulans mutant (BWB26A) deficient in O-glycosylation caused an increase in the number of secretory vesicles and changes in protein secretion. However, the secretory proteins, primarily O-mannosylated glucoamylase and N-glycosylated invertase, were mainly trapped in the periplasmic space. Different glycoforms of invertase were found insite the cells, in the periplasmic space and in the cultivation medium. Our data point to the importance of the cell wall as a barrier in protein secretion.
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