磷脂生物合成的CDP-胆碱途径中的突变绕过了对必需磷脂转移蛋白的需求。
Mutations in the CDP-choline pathway for phospholipid biosynthesis bypass the requirement for an essential phospholipid transfer protein.
作者信息
Cleves A E, McGee T P, Whitters E A, Champion K M, Aitken J R, Dowhan W, Goebl M, Bankaitis V A
机构信息
Department of Microbiology, University of Illinois, Urbana-Champaign 61801.
出版信息
Cell. 1991 Feb 22;64(4):789-800. doi: 10.1016/0092-8674(91)90508-v.
Abstract
SEC14p is the yeast phosphatidylinositol (PI)/phosphatidylcholine (PC) transfer protein, and it effects an essential stimulation of yeast Golgi secretory function. We now report that the SEC14p localizes to the yeast Golgi and that the SEC14p requirement can be specifically and efficiently bypassed by mutations in any one of at least six genes. One of these suppressor genes was the structural gene for yeast choline kinase (CKI), disruption of which rendered the cell independent of the normally essential SEC14p requirement. The antagonistic action of the CKI gene product on SEC14p function revealed a previously unsuspected influence of biosynthetic activities of the CDP-choline pathway for PC biosynthesis on yeast Golgi function and indicated that SEC14p controls the phospholipid content of yeast Golgi membranes in vivo.
摘要
SEC14p是酵母磷脂酰肌醇（PI）/磷脂酰胆碱（PC）转移蛋白，它对酵母高尔基体分泌功能有至关重要的刺激作用。我们现在报告，SEC14p定位于酵母高尔基体，并且至少六个基因中的任何一个发生突变都可以特异性且有效地绕过对SEC14p的需求。其中一个抑制基因是酵母胆碱激酶（CKI）的结构基因，其破坏使细胞不再依赖通常必需的SEC14p。CKI基因产物对SEC14p功能的拮抗作用揭示了PC生物合成的CDP-胆碱途径的生物合成活性对酵母高尔基体功能有先前未被怀疑的影响，并表明SEC14p在体内控制酵母高尔基体膜的磷脂含量。
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