植物质膜H(+) -ATP酶的C末端缺失分析：以酵母作为溶质跨植物质膜运输的模型系统
C-terminal deletion analysis of plant plasma membrane H(+)-ATPase: yeast as a model system for solute transport across the plant plasma membrane.
作者信息
Regenberg B, Villalba J M, Lanfermeijer F C, Palmgren M G
机构信息
Department of Plant Biology, Royal Veterinary and Agricultural University, Copenhagen, Denmark.
出版信息
Plant Cell. 1995 Oct;7(10):1655-66. doi: 10.1105/tpc.7.10.1655.
Abstract
The plasma membrane proton pump (H(+)-ATPase) energizes solute uptake by secondary transporters. Wild-type Arabidopsis plasma membrane H(+)-ATPase (AHA2) and truncated H(+)-ATPase lacking 38, 51, 61, 66, 77, 92, 96, and 104 C-terminal amino acids were produced in yeast. All AHA2 species were correctly targeted to the yeast plasma membrane and, in addition, accumulated in internal membranes. Removal of 38 C-terminal residues from AHA2 produced a high-affinity state of plant H(+)-ATPase with a low Km value (0.1 mM) for ATP. Removal of an additional 12 amino acids from the C terminus resulted in a significant increase in molecular activity of the enzyme. There was a close correlation between molecular activity of the various plant H(+)-ATPase species and their ability to complement mutants of the endogenous yeast plasma membrane H(+)-ATPase (pma1). This correlation demonstrates that, at least in this heterologous host, activation of H(+)-ATPase is a prerequisite for proper energization of the plasma membrane.
摘要
质膜质子泵（H(+)-ATP酶）为次级转运蛋白的溶质摄取提供能量。在酵母中表达了野生型拟南芥质膜H(+)-ATP酶（AHA2）以及缺失38、51、61、66、77、92、96和104个C末端氨基酸的截短型H(+)-ATP酶。所有AHA2种类都能正确定位于酵母质膜，此外，还在内膜中积累。从AHA2中去除38个C末端残基产生了植物H(+)-ATP酶的高亲和力状态，对ATP的Km值较低（0.1 mM）。从C末端再去除另外12个氨基酸导致该酶的分子活性显著增加。各种植物H(+)-ATP酶种类的分子活性与其补充内源性酵母质膜H(+)-ATP酶（pma1）突变体的能力之间存在密切相关性。这种相关性表明，至少在这种异源宿主中，H(+)-ATP酶的激活是质膜正常供能的先决条件。
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