大麦凝集素液泡靶向信号内功能元件的测定
Determination of the functional elements within the vacuolar targeting signal of barley lectin.
作者信息
Dombrowski J E, Schroeder M R, Bednarek S Y, Raikhel N V
机构信息
Department of Energy Plant Research Laboratory, Michigan State University, East Lansing 48824-1312.
出版信息
Plant Cell. 1993 May;5(5):587-96. doi: 10.1105/tpc.5.5.587.
Abstract
We have previously demonstrated that the carboxyl-terminal propeptide of barley lectin is both necessary and sufficient for protein sorting to the plant vacuole. Specific mutations were constructed to determine which amino acid residues or secondary structural determinants of the carboxyl-terminal propeptide affect proper protein sorting. We have found that no consensus sequence or common structural determinants are required for proper sorting of barley lectin to the vacuole. However, our analysis demonstrated the importance of hydrophobic residues in vacuolar targeting. In addition, at least three exposed amino acid residues are necessary for efficient sorting. Sorting was disrupted by the addition of two glycine residues at the carboxyl-terminal end of the targeting signal or by the translocation of the glycan to the carboxy terminus of the propeptide. These results suggest that some components of the sorting apparatus interact with the carboxy terminus of the propeptide.
摘要
我们之前已经证明，大麦凝集素的羧基末端前肽对于蛋白质分选到植物液泡既是必需的也是充分的。构建了特定突变以确定羧基末端前肽的哪些氨基酸残基或二级结构决定因素会影响正确的蛋白质分选。我们发现，将大麦凝集素正确分选到液泡并不需要共有序列或共同的结构决定因素。然而，我们的分析证明了疏水残基在液泡靶向中的重要性。此外，至少三个暴露的氨基酸残基对于有效分选是必需的。在靶向信号的羧基末端添加两个甘氨酸残基，或者将聚糖转移到前肽的羧基末端，都会破坏分选。这些结果表明，分选装置的某些组分与前肽的羧基末端相互作用。
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