U Lenart

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

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A. Janik

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Joanna S. Kruszewska

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Grażyna Palamarczyk

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Mateusz Juchimiuk

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Grazyna B. Palamarczyk

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Vladimı́r Farkaš

Slovak Academy of Sciences

Peter Magdolen

Comenius University Bratislava

Monika Niewiadomska

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Jana Haplová

Slovak Academy of Sciences

Cooperative Institutions

Institute of Biochemistry and Biophysics, Polish Academy of Sciences

Polish Academy of Sciences

Slovak Academy of Sciences

Institute of Chemistry of the Slovak Academy of Sciences

WSB University

Medical University of Silesia

Zakład Doświadczalny Instytutu Zootechniki

National Research Institute of Animal Production

Szpital Uniwersytecki w Krakowie

Jagiellonian University

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

Acta Biochimica Polonica (1995)

U Lenart Jana Haplová Peter Magdolen Vladimı́r Farkaš Grażyna Palamarczyk

The membrane-bound sterolglucoside synthase from the yeast Saccharomyces cerevisiae has been solubilized by nonionic detergent, Nonidet P-40, Triton X-100, and partially purified by DEAE-cellulose column chromatography and ammonium sulfate fractionation. SDS/PAGE of the purified fraction revealed the presence of two protein bands of molecular mass 66 kDa and 54 kDa. In an attempt to identify further the polypeptide chain of sterolglucoside synthase, the partially purified enzyme was treated with [di-125I]-5-[3-(p-azidosalicylamide)]allyl-UDPglucose, a photoactive analogue of UDP glucose, which is a substrate for this enzyme. Upon photolysis the 125I-labeled probe was shown to link covalently to the 66 kDa protein. The photoinsertion was competed out by the presence of unlabeled UDPglucose thus suggesting that this protein contains substrate binding site for UDPglucose. Since photoinsertion of the probe to protein of 66 kDa correlates with the molecular mass of the protein visualized upon enzyme purification we postulate that the 66 kDa protein is involved in sterolglucoside synthesis in yeast.

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Chaps

10.18388/abp.1995_4657

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Citations (4)

Glycosylation defects corrected by the changes in GDPmannose level.

Acta Biochimica Polonica (1999)

Joanna S. Kruszewska A. Janik U Lenart Grażyna Palamarczyk

GDPMan is a key substrate in glycoprotein formation. This is especially true for lower eukaryotes where, in addition to the involvement in N-glycan biosynthesis and GPI-anchor formation, GDPMan takes part in the process which is unique for yeast and fungi i.e. O-mannosylation. Several lines of evidence have been presented that the level of GDPMan affects the process occurring in the Golgi compartment i.e. the elongation of outer mannose chain of glycoproteins in Saccharomyces cerevisiae. Results from our laboratory indicate that the availability of GDPMan affects also the early steps of glycoprotein formation ascribed to the endoplasmic reticulum, i.e. assembly of the dolichol-linked oligosaccharide as well as mannosyl-phosphodolichol (MPD) formation. The biochemical basis of carbohydrate deficient glycoprotein syndrome, a severe neurological disorder related to the GDPMan deficiency, is also discussed.

Dolichol

Oligosaccharide

10.18388/abp.1999_4165

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Candida albicans; exploring glycosylation pathway in the search of targets for antimicrobial agents and yeast to hyphae transition.

Medical Research Archives (2019)

A. Janik Mateusz Juchimiuk Monika Niewiadomska U Lenart Joanna S. Kruszewska

Microbial cell wall is mostly synthesized by the glycosylated proteins with the distinct enzymatic activity. In this review we have concentrated on the description of the certain steps of glycosylation and their effect on the cell wall integrity and yeast to hyphae transition, the process enhancing the pathogenic properties of C.albicans. The glycoproteins play an invaluable role in C. albicans virulence and they modulate adhesive, invasive, morphogenetic and immune stimulating properties of the pathogen as well as its susceptibility to the antifungal agents. Therefore, understanding of C. albicans glycobiology might let us expand the arsenal in the war against fungal enemies. The early stages of N-, O-glycans and GPI-anchor synthesis requires dolichol - the lipid carrier of sugar residues. Diminished supply of dolichol causes series of defects in C. albicans cells, among which aberrant protein glycosylation is the most evident. Furthermore, the relations between the cell wall composition and integrity, resistance to some antifungal and cell wall disturbing agents and dolichol dependent glycosylation are observed. Moreover relevance of these reactions for the morphological differentiation of C.albicans is described.

Dolichol

Glycobiology

10.18103/mra.v7i9.1968

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