The yeast cell fusion protein FUS1 is O-glycosylated and spans the plasma membrane.
The yeast cell fusion protein FUS1 is O-glycosylated and spans the plasma membrane.
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酵母细胞融合蛋白 FUS1 被 O-糖基化并跨越质膜。
DOI：
10.1073/pnas.86.24.9916
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发表时间：
1989
影响因子：
11.1
通讯作者：
Fink,GR
中科院分区：
文献类型：
--
作者：
Trueheart,J;Fink,GR
先前的工作表明，酿酒酵母接合过程中有效的细胞融合需要由 FUS1 编码的信息素诱导的表面蛋白。我们表明，FUS1 蛋白在 SDS/聚丙烯酰胺凝胶上迁移，表观分子量为 80 kDa，尽管根据基因编码能力预测该质量为 58 kDa。这种差异是由于存在连接到蛋白质氨基末端簇状丝氨酸和苏氨酸上的 O-连接甘露糖寡糖造成的。甘露糖的添加在早期分泌突变体 sec53 中被完全取消，在晚期内质网阻断的 sec18 中减弱，并且在 sec7 中不受影响，后者在分泌的晚期被阻断。膜分级分离和蛋白酶保护实验表明，FUS1 跨越质膜，其糖基化氨基末端伸入周质空间。
Previous work has shown that efficient cell fusion during conjugation in Saccharomyces cerevisiae requires a pheromone-induced surface protein encoded by FUS1. We show that the FUS1 protein migrates on SDS/polyacrylamide gels with an apparent molecular mass of 80 kDa, although the mass is predicted to be 58 kDa from the gene coding capacity. This discrepancy results from the presence of O-linked mannose oligosaccharides attached to the clustered serines and threonines at the amino terminus of the protein. The addition of mannose is completely abolished in the early secretory mutant sec53, attenuated in the late-endoplasmic reticulum-blocked sec18, and unaffected in sec7, which is blocked late in the Golgi phase of secretion. Membrane fractionation and protease protection experiments indicate that FUS1 spans the plasma membrane, with its glycosylated amino terminus projecting into the periplasmic space.