O-Glycosylation of Proteins by Membrane Fractions of Trichoderma reesei QM 9414

Kruszewska, Joanna S.; Messner, Rudolf; Kubicek, Christian P.; Palamarczyk, Grażyna

doi:10.1099/00221287-135-2-301

Cited by 26 publications

(35 citation statements)

References 24 publications

(12 reference statements)

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“…Data given are from a single experiment, but replicate experiments yielded essentially the same result. which coincides with previous findings (Kruszewska et al, 1989).…”

Section: Table I Mannosyl Transfer From Gdp-[ U-l4c]mannose To Lipidsupporting

confidence: 82%

“…In order to find out whether other enzymes involved in 0-glycosylation might exhibit increased activities in mycelia after supplementation by choline or Tween 80, the incubation system for the assay of Dol-P-Man synthase was 'chased' with cold GDP-mannose and the reaction was allowed to proceed in the presence of manganese ions (Kruszewska et al, 1989). The results are shown in Table 3 : pulsing with GDP-mannose led to a moderate increase in labelling of protein, which occurred at a comparable rate with membrane preparations isolated under various conditions.…”

Section: Mannosyl Transfer From Gdp-[ U-4c]mannose To Endogenous Proteinmentioning

confidence: 99%

“…A membrane fraction, capable of carrying out 0-glycosylation, was isolated from the fungus by homogenization of mycelia with glass beads and centrifugation as described previously (Kruszewska et al, 1989).…”

Section: Cell Fractionationmentioning

confidence: 99%

“…We have recently shown that 0-glycosylation in T. reesei (Kruszewska et al, 1989) proceeds in a similar way to that in yeasts (Tanner & Lehle, 1987), and may be controlled at the level of Dol-P or GDP-mannose supply.…”

Section: Introductionmentioning

confidence: 99%

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Stimulation of exoprotein secretion by choline and Tween 80 in Trichoderma reesei QM 9414 correlates with increased activities of dolichol phosphate mannose synthase

Kruszewska

Palamarczyk

Kubicek

1990

Journal of General Microbiology

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~Addition of choline (20 mM) or Tween 80 (0.06 %) to the culture medium of Trichoderma reesei QM 9414 increased (a) the secretion of protein under both carbon-catabolite-repressed and -derepressed conditions, and (b) cellulase secretion under carbon-catabolite-derepressed conditions. In contrast, no stimulation by choline or Tween 80 was observed with the hypersecretory strain T. reesei RUT C-30. In view of the obligatory role of 0-glycosylation in protein secretion by this fungus, an investigation was made into the effects on this process of choline and Tween 80.A membrane preparation was isolated from both strains of T. reesei and used to assay enzymes involved in 0-glycosylation. Significant differences were observed with respect to the activity of dolichol phosphate mannose (Dol-P-Man) synthase only. Strain QM 9414, grown on media supplemented with choline or Tween 80 exhibited a two-to threefold higher activity of Dol-P-Man synthase compared to a control lacking these supplements. This stimulatory effect was observed during growth under both carbon-catabolite-repressed and -derepressed conditions. In contrast, strain RUT C-30 exhibited decreased activities of Dol-P-Man synthase when grown in media supplemented with choline. Choline had no effect on Dol-P-Man synthase in vifro, whereas Tween 80 decreased the activity. Thus the effect of Tween 80 or choline on protein secretion by T. reesei may be due to a stimulation of formation and/or activity of Dol-P-Man synthase, thereby elevating the level of 0-glycosylation and protein secretion.

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“…Data given are from a single experiment, but replicate experiments yielded essentially the same result. which coincides with previous findings (Kruszewska et al, 1989).…”

Section: Table I Mannosyl Transfer From Gdp-[ U-l4c]mannose To Lipidsupporting

confidence: 82%

Section: Mannosyl Transfer From Gdp-[ U-4c]mannose To Endogenous Proteinmentioning

confidence: 99%

Section: Cell Fractionationmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Stimulation of exoprotein secretion by choline and Tween 80 in Trichoderma reesei QM 9414 correlates with increased activities of dolichol phosphate mannose synthase

Kruszewska

Palamarczyk

Kubicek

1990

Journal of General Microbiology

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“…The activity of Dpm1p or Alg7p or Alg14p proteins was measured in the membrane fraction, obtained as for cis-prenyltransferase, according to Kruszewska et al (1989) with GDP-( 14 C) mannose (296 Ci/mol; Amersham) or UDP-( 14 C) Nacetylglucosamine (235 Ci/mol).…”

Section: Dolpman or Dolppgnac 2 Synthase Activity Assaymentioning

confidence: 99%

Dissecting the role of dolichol in cell wall assembly in the yeast mutants impaired in early glycosylation reactions

Orłowski

Machula

Janik

et al. 2007

Yeast

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Evidence is presented that temperature-sensitive Saccharomyces cerevisiae mutants, impaired in dolichol kinase (Sec59p) or dolichyl phosphate mannose synthase (Dpm1p) activity have an aberrant cell wall composition and ultrastructure. The mutants were oversensitive to Calcofluor white, an agent interacting with the cell wall chitin. In accordance with this, chemical analysis of the cell wall alkali-insoluble fraction indicated an increased amount of chitin and changes in the quantity of β1,6-and β1,3-glucan in sec59-1 and dpm1-6 mutants. In order to unravel the link between the formation of dolichyl phosphate and dolichyl phosphate mannose and the cell wall assembly, we screened a yeast genomic library for a multicopy suppressors of the thermosensitive phenotype. The RER2 and SRT1 genes, encoding cis-prenyltransferases, were isolated. In addition, the ROT1 gene, encoding protein involved in β1,6-glucan synthesis (Machi et al., 2004) and protein folding (Takeuchi et al., 2006) acted as a multicopy suppressor of the temperature-sensitive phenotype of the sec59-1 mutant. The cell wall of the mutants and of mutants bearing the multicopy suppressors was analysed for carbohydrate and mannoprotein content. We also examined the glycosylation status of the plasma membrane protein Gas1p, a β1,3-glucan elongase, and the degree of phosphorylation of the Mpk1/Slt2 protein, involved in the cell wall integrity pathway.

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Mannosyl-phospho-dolichol synthase from Trichoderma reesei is activated by protein kinase dependent phosphorylation in vitro

Kruszewska

1991

FEMS Microbiology Letters

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Summary Preincubation of microsomes from Trichoderma reesei QM 9414 with the catalytic subunit of cyclic AMP dependent protein kinase from bovine heart resulted in increased activity of the mannosylphospho‐dolichol synthase (EC 2.4.1.83, ‘Dol‐P‐Man synthase’) present in the membranes. This effect decreased upon subsequent treatment of the microsomes with alkaline phosphatase. SDS‐PAGE of microsomal proteins indicated the presence of a strong band at 32 kDa, which corresponds to the size of yeast Dol‐P‐Man synthase. Fluorography of microsomal proteins, after incubation with [γ‐32P]ATP and protein kinase, revealed the incorporation of 32P into this 32‐kDa as well as several other microsomal proteins. Dol‐P‐Man synthase activity, assayed at various times of growth, correlated with the rise and fall of the cyclic AMP pool in T. reesei. Addition of extracellular dibutyryl cyclic AMP and theophyllin, however, did not elevate the internal cyclic AMP pool in the fungus, and did not cause an effect on Dol‐P‐Man synthase activity.

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O-Glycosylation of Proteins by Membrane Fractions of Trichoderma reesei QM 9414

Cited by 26 publications

References 24 publications

Stimulation of exoprotein secretion by choline and Tween 80 in Trichoderma reesei QM 9414 correlates with increased activities of dolichol phosphate mannose synthase

Stimulation of exoprotein secretion by choline and Tween 80 in Trichoderma reesei QM 9414 correlates with increased activities of dolichol phosphate mannose synthase

Dissecting the role of dolichol in cell wall assembly in the yeast mutants impaired in early glycosylation reactions

Mannosyl-phospho-dolichol synthase from Trichoderma reesei is activated by protein kinase dependent phosphorylation in vitro

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