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Wyszukujesz frazę "glycosylation" wg kryterium: Temat


Wyświetlanie 1-3 z 3
Tytuł:
Alterations in protein secretion caused by metabolic engineering of glycosylation pathways in fungi
Autorzy:
Kruszewska, Joanna
Perlińska-Lenart, Urszula
Górka-Nieć, Wioletta
Orłowski, Jacek
Zembek, Patrycja
Palamarczyk, Grażyna
Powiązania:
https://bibliotekanauki.pl/articles/1040697.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
protein secretion
Trichoderma
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2008, 55, 3; 447-456
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Protein production and secretion in an Aspergillus nidulans mutant impaired in glycosylation.
Autorzy:
Perlińska-Lenart, Urszula
Kurzątkowski, Wiesław
Janas, Piotr
Kopińska, Agnieszka
Palamarczyk, Grażyna
Kruszewska, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1041477.pdf
Data publikacji:
2005
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
glycosylation
protein secretion
DPM1 gene
Aspergillus
dolichylphosphate mannose synthase
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2005, 52, 1; 195-205
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
Tytuł:
Disruption of Trichoderma reesei gene encoding protein O-mannosyltransferase I results in a decrease of the enzyme activity and alteration of cell wall composition
Autorzy:
Górka-Nieć, Wioletta
Pniewski, Michał
Kania, Anna
Perlińska-Lenart, Urszula
Palamarczyk, Grażyna
Kruszewska, Joanna
Powiązania:
https://bibliotekanauki.pl/articles/1040737.pdf
Data publikacji:
2008
Wydawca:
Polskie Towarzystwo Biochemiczne
Tematy:
Trichoderma reesei
pmt1 gene disruption
protein glycosylation
cell wall composition
Opis:
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.
Źródło:
Acta Biochimica Polonica; 2008, 55, 2; 251-259
0001-527X
Pojawia się w:
Acta Biochimica Polonica
Dostawca treści:
Biblioteka Nauki
Artykuł
    Wyświetlanie 1-3 z 3

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