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Bacitracin Inhibits the Synthesis of Lipid-linked Saccharides and Glycoproteins in Plants
Author(s) -
Mary C. Ericson,
John T. Gafford,
Alan D. Elbein
Publication year - 1978
Publication title -
plant physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.62.3.373
Subject(s) - bacitracin , mannose , biochemistry , glycosylation , chemistry , glycoprotein , dolichol , lysine , cell wall , tunicamycin , enzyme , biosynthesis , antibiotics , amino acid , endoplasmic reticulum , unfolded protein response
The particulate enzyme fraction from mung bean (Phaseolus aureus) seedlings catalyzes the incorporation of mannose from GDP-[(14)C]mannose into mannosyl-phosphoryl-dolichol and of N-acetylglucosamine from UDP-[(3)H]N-acetylglucosamine into N-acetylglucosamine-pyrophosphoryl-polyisoprenol. Bacitracin inhibits the transfer of both of these sugars into the lipid-linked saccharides with 50% inhibition being observed at 5 mm bacitracin. This antibiotic did not inhibit the transfer of glucose from UDP-[(14)C]glucose into steryl glucosides or the incorporation of glucose into a cell wall glucan. Bacitracin also inhibited the in vivo incorporation of [(14)C]mannose into mannosyl-phosphoryl-dolichol and into glycoprotein by carrot (Daucus carota) slices. While bacitracin also inhibited the incorporation of lysine into proteins by these slices, protein synthesis was less sensitive than glycosylation. Thus at 2 mm bacitracin glycosylation was inhibited 92%, while protein synthesis was inhibited only 50%.

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