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1
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Dolichols and enzymatic formation of dolichyl phosphate sugars in the thymus of mice on neoplastic transformation

100%
Szkopińska A., Palamarczyk G., Chojnacki T.
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vol. 32
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issue 1
63-70
2
Content available remote

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
3
Content available remote

Evidence for the involvement of a 66 kDa membrane protein in the synthesis of sterolglucoside in Saccharomyces cerevisiae

88%
Lenart U., Haplova J., Magdolen P., Farkas V., Palamarczyk G.
Acta Biochimica Polonica
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1995
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vol. 42
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issue 2
269-274
4
Content available remote

Glycosylation defects corrected by the changes in GDPmannose level

88%
Kruszewska J., Janik A., Lenart U., Palamarczyk G.
Acta Biochimica Polonica
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1999
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vol. 46
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issue 2
315-324
5
Content available remote

Rsp5 ubiquitin ligase affects isoprenoid pathway and cell wall organization in S. cerevisiae.

76%
Kamińska J., Kwapisz M., Grabińska K., Orłowski J., Boguta M., Palamarczyk G., Żołądek T.
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2005
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vol. 52
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issue 1
207-220
EN
Dimethylallyl diphosphate, an isomer of isopentenyl diphosphate, is a common substrate of Mod5p, a tRNA modifying enzyme, and the farnesyl diphosphate synthase Erg20p, the key enzyme of the isoprenoid pathway. rsp5 mutants, defective in the Rsp5 ubiquitin-protein ligase, were isolated and characterized as altering the mitochondrial/cytosolic distribution of Mod5p. To understand better how competition for the substrate determines the regulation at the molecular level, we analyzed the effect of the rsp5-13 mutation on Erg20p expression. The level of Erg20p was three times lower in rsp5-13 compared to the wild type strain and this effect was dependent on active Mod5p. Northern blot analysis indicated a regulatory role of Rsp5p in ERG20 transcription. ERG20 expression was also impaired in pkc1Δ lacking a component of the cell wall integrity signaling pathway. Low expression of Erg20p in rsp5 cells was accompanied by low level of ergosterol, the main end product of the isoprenoid pathway. Additionally, rsp5 strains were resistant to nystatin, which binds to ergosterol present in the plasma membrane, and sensitive to calcofluor white, a drug destabilizing cell wall integrity by binding to chitin. Furthermore, the cell wall structure appeared abnormal in most rsp5-13 cells investigated by electron microscopy and chitin level in the cell wall was increased two-fold. These results indicate that Rsp5p affects the isoprenoid pathway which has important roles in ergosterol biosynthesis, protein glycosylation and transport and in this way may influence the composition of the plasma membrane and cell wall.
6
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Functional relationships between the Saccharomyces cerevisiae cis-prenyltransferases required for dolichol biosynthesis.

76%
Grabińska K., Sosińska G., Orłowski J., Swiezewska E., Berges T., Karst F., Palamarczyk G.
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2005
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vol. 52
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issue 1
221-232
EN
In the yeast Saccharomyces cerevisiae the RER2 and SRT1 genes encode Rer2 and Srt1 proteins with cis-prenyltransferase (cis-PT-ase) activity. Both cis-PT-ases utilize farnesyl diphosphate (FPP) as a starter for polyprenyl diphosphate (dolichol backbone) formation. The products of the Rer2 and Srt1 proteins consist of 14-17 and 18-23 isoprene units, respectively. In this work we demonstrate that deletion or overexpression of SRT1 up-regulates the activity of Rer2p and dolichol content. However, upon overexpression of SRT1, preferential synthesis of longer-chain dolichols and a decrease in the amount of the shorter species are observed. Furthermore, overexpression of the ERG20 gene (encoding farnesyl diphosphate synthase, Erg20p) induces transcription of SRT1 mRNA and increases the levels of mRNA for RER2 and DPM1 (dolichyl phosphate mannose synthase, Dpm1p). Subsequently the enzymatic activity of Rer2p and dolichol content are also increased. However, the amount of Dpm1p or its enzymatic activity remain unchanged.
7
Content available remote

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.
8
Content available remote

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.
9
Content available remote

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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