Tunicamycin — An inhibitor of yeast glycoprotein synthesis

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Abstract

Tunicamycin, a glucosamine-containing antibiotic, halted synthesis of the external glycoproteins invertase, acid phosphatase and mannan by yeast protoplasts within 30 min; formation of two intracellular proteins, alpha-glucosidase and alkaline phosphatase, and of glucan continued at the control rate for at least 60–80 min. No accumulation of mannan-free acid phosphatase or invertase was evident in treated cells. Utilization of hexoses and incorporation of 14C-amino acids into protein were not affected. Incorporation of 3H-glucosamine into trichloroacetic acid-insoluble products was only partially reduced. In yeast tunicamycin acts primarily as an inhibitor of glycoprotein synthesis and not of general glucosamine metabolism.

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    We also assess the robustness of MILPIG using a panel of normal (12C) and isotope-labeled (13C) glycan mixtures from differentially labeled yeast cells. Finally, we examined the difference in N-linked glycans expression under in normal and tunicamycin-treated cells using MILPIG approach [37,38]. Collectively, our results corroborate that MILPIG has an excellent potential for relative glycomics to study glycan changes in physiological conditions in cell culture.

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