Tunicamycin inhibition of (3H) glucosamine incorporation into yeast glycoproteins: binding of tunicamycin and interaction with phospholipids.
Tunicamycin inhibition of (3H) glucosamine incorporation into yeast glycoproteins: binding of tunicamycin and interaction with phospholipids.
复制标题
衣霉素抑制 (3H) 葡萄糖胺掺入酵母糖蛋白：衣霉素的结合以及与磷脂的相互作用。
DOI：
10.1016/0003-9861(76)90110-7
复制
发表时间：
1976
影响因子：
3.9
通讯作者：
O. Lampen
中科院分区：
文献类型：
--
作者：
S. Kuo;O. Lampen
在有能量来源的情况下，放线菌菌株1016的原生质体吸收[3 H]葡糖胺;选择甘露糖以使随机化最小化。它主要以UDP-N-乙酰基[3 H]葡糖胺沿着少量[3 H]葡糖胺6-磷酸的形式在可溶性细胞内池中积累。10 μg/ml的抗生素衣霉素（TM）不影响这些代谢物的水平或抑制N-乙酰葡糖胺聚合物几丁质的形成，但确实阻止[3 H]葡糖胺掺入甘露聚糖肽和转化酶的合成。TM似乎抑制糖蛋白生物合成所必需的N-乙酰葡糖胺基转移酶。[3 H]TM的结合反映了其与质膜组分的结合。该物质可以通过用氯仿/甲醇萃取以未改变的形式回收。若同时加入0.2%磷脂酰胆碱或磷脂酰丝氨酸，则[3 H]TM的结合大大减少，TM对原生质体的抑制作用被阻止，但20 min后加入磷脂，虽然约80%的结合[3 H]TM被去除，但仍不能消除TM对原生质体的抑制作用。TM与亲脂性膜组分相互作用，并抑制糖蛋白合成。
Protoplasts ofSaccharomycesstrain 1016 took up [3H]glucosamine in the presence of an energy source; mannose was chosen to minimize randomization. It accumulated in the soluble intracellular pool primarily as UDP-N-acetyl[3H]glucosamine along with a small amount of [3H]glucosamine 6-phosphate. The antibiotic tunicamycin (TM) at 10 μg/ml did not affect the levels of these metabolites or inhibit the formation of theNacetylglucosamine polymer, chitin, but did prevent the incorporation of [3H]glucosamine into mannan peptides and the synthesis of invertase.In vitroincorporation of [14C]mannose from GDP-[14C]mannose into mannan in a membrane preparation was not sensitive to 100 μg of TM/ml. TM appears to inhibit anN-acetylglucosaminyl transferase essential for glycoprotein biosynthesis. Binding of [3H]TM reflects its association with the plasma membrane fraction. This material could be recovered in an unaltered form by extraction with chloroform/methanol. If 0.2% phosphatidyl choline or phosphatidyl serine was added simultaneously with the [3H]TM, the binding of [3H]TM was greatly reduced, and the inhibitory effects of TM on protoplasts were prevented; however, addition of phospholipid 20 min later did not eliminate the inhibition, although about 80% of the bound [3H]TM was removed. TM interacts with lipophilic membrane components as well as inhibiting glycoprotein synthesis.