Sorting signals within the Saccharomyces cerevisiae sporulation-specific dityrosine transporter, Dtr1p, C terminus promote Golgi-to-prospore membrane transport.
Sorting signals within the Saccharomyces cerevisiae sporulation-specific dityrosine transporter, Dtr1p, C terminus promote Golgi-to-prospore membrane transport.
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酿酒酵母孢子形成特异性二酪氨酸转运蛋白、Dtr1p、C 末端内的分选信号促进高尔基体到原生孢子膜的转运。
DOI：
10.1128/ec.00151-08
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发表时间：
2008
期刊：
影响因子：
--
通讯作者：
Engebrecht,JoAnne
中科院分区：
文献类型：
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作者：
Morishita,Masayo;Engebrecht,JoAnne
在酿酒酵母（Saccharomycescerevisiae）的孢子形成过程中，形成孢子壁最外层所需的双酪氨酸转运蛋白Dtr 1 p被特异性表达并转运至原孢子膜（一种新型的双脂双层膜）。Dtr 1 p由572个氨基酸组成，具有预测的N-和C-末端胞质延伸和12个跨膜结构域。缺失最大内部胞质环的DTR 1 P被困在有丝分裂细胞和诱导形成孢子的细胞的内质网中。删除的羧基15个氨基酸，但不是N-末端延伸的DTR 1 P，导致蛋白质，未能本地化的前孢子膜，而是观察到在细胞质斑点。puncta与acis-Golgi标记共定位，表明Dtr 1 p缺失最后15个氨基酸被困在早期的高尔基体隔室中。C-末端10个氨基酸的缺失导致定位于前孢子膜的蛋白质具有延迟并积累在与atrans-Golgi标记部分共定位的细胞质点中。全长Dtr 1 p和Dtr 1 p缺失的最后10个氨基酸在营养细胞定位到质膜和液泡中表达，而Dtr 1 p删除的羧基末端15个氨基酸仅在液泡中观察到，这表明运输到原孢子膜是由不同的信号介导的，从那些指定质膜定位。功能转移实验表明，羧基跨膜结构域和C-末端尾是重要的高尔基复合体的原孢子膜运输。
During sporulation inSaccharomyces cerevisiae, the dityrosine transporter Dtr1p, which is required for formation of the outermost layer of the spore wall, is specifically expressed and transported to the prospore membrane, a novel double-lipid-bilayer membrane. Dtr1p consists of 572 amino acids with predicted N- and C-terminal cytoplasmic extensions and 12 transmembrane domains. Dtr1p missing the largest internal cytoplasmic loop was trapped in the endoplasmic reticulum in both mitotically dividing cells and cells induced to sporulate. Deletion of the carboxyl 15 amino acids, but not the N-terminal extension of Dtr1p, resulted in a protein that failed to localize to the prospore membrane and was instead observed in cytoplasmic puncta. The puncta colocalized with acis-Golgi marker, suggesting that Dtr1p missing the last 15 amino acids was trapped in an early Golgi compartment. Deletion of the C-terminal 10 amino acids resulted in a protein that localized to the prospore membrane with a delay and accumulated in cytoplasmic puncta that partially colocalized with atrans-Golgi marker. Both full-length Dtr1p and Dtr1p missing the last 10 amino acids expressed in vegetative cells localized to the plasma membrane and vacuoles, while Dtr1p deleted for the carboxyl-terminal 15 amino acids was observed only at vacuoles, suggesting that transport to the prospore membrane is mediated by distinct signals from those that specify plasma membrane localization. Transfer-of-function experiments revealed that both the carboxyl transmembrane domain and the C-terminal tail are important for Golgi complex-to-prospore membrane transport.