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1

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

100%

Kruszewska J. S., Perlińska-Lenart U., Palamarczyk G.

Acta Biochimica Polonica

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1996

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vol. 43

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issue 2

397-401

2

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

76%

Kruszewska J. S., Perlińska-Lenart U., Górka-Nieć W., Orłowski J., Zembek P., Palamarczyk G.

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2008

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vol. 55

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issue 3

447-456

EN

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.

3

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

76%

Górka-Nieć W., Pniewski M., Kania A., Perlińska-Lenart U., Palamarczyk G., Kruszewska J.

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2008

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vol. 55

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issue 2

251-259

EN

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 pmt1 gene in Trichoderma caused a significant decrease in the total activity of protein O-mannosyltransferases. Moreover, disruption of the pmt1 gene 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 pmt1 gene 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

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

76%

Perlińska-Lenart U., Kurzątkowski W., Janas P., Kopińska A., Palamarczyk G., Kruszewska J. S.

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2005

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vol. 52

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issue 1

195-205

EN

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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4 Acta Biochimica Polonica

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1 Kruszewska J.

1 Kurzątkowski W.

1 Orłowski J.

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1 Zembek P.

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

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

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

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