Proteins in the early Golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p
Proteins in the early Golgi compartment of Saccharomyces cerevisiae immunoisolated by Sed5p
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DOI：
10.1016/s0014-5793(00)01268-0
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发表时间：
2000-03-10
期刊：
影响因子：
3.5
通讯作者：
Yoda, K
中科院分区：
文献类型：
--
作者：
Cho, JH;Noda, Y;Yoda, K
酵母tSNARE Sed 5 p被认为在其细胞内循环的稳定状态下主要驻留在早期高尔基体隔室中。为了更好地理解这个区室，我们免疫分离了表面上具有Sed 5 p的膜亚组分（Sed 5囊泡）。免疫印迹研究搁置，相当大的部分（20-30%）的高尔基甘露糖基转移酶（Mnt 1 p，Van 1 p和Mnn 9 p）同时回收，而后期高尔基体（Kex 2 p）或内质网（Sec 71 p）蛋白几乎被排除在外。通过考马斯蓝染色可检测的多肽的N-末端序列表明，Sed 5囊泡的主要组分包括Anp 1 p、Emp 24 p、Erv 25 p、Erp 1 p、Ypt 52 p和一种功能未知的推定膜蛋白（Yml 067 c）。(C)2000年欧洲生物化学学会联合会。
The yeast tSNARE Sed5p is considered to mainly reside in the early Golgi compartment at the steady state of its intracellular cycling. To better understand this compartment, we immunoisolated a membrane subfraction having Sed5p on the surface (the Sed5 vesicles). Immunoblot studies shelved that considerable portions (20-30%) of the Golgi mannosyltransferases (Mnt1p, Van1p, and Mnn9p) were simultaneously recovered while the late Golgi (Kex2p) or endoplasmic reticulum (Sec71p) proteins were almost excluded. The N-terminal sequences of the polypeptides detectable by Coomassie blue staining indicated that the prominent components of the Sed5 vesicles include Anp1p, Emp24p, Erv25p, Erp1p, Ypt52p, and a putative membrane protein of unknown function (Yml067c). (C) 2000 Federation of European Biochemical Societies.