Physiological function of Na^+/K^+ transporters from bacteria and plants

细菌和植物Na^/K^转运蛋白的生理功能

• 批准号: 13660088
• 负责人: UOZUMI Nobuyuki
• 金额: $ 2.3万
• 依托单位: NAGOYA UNIVERSITY
• 依托单位国家: 日本
• 项目类别: Grant-in-Aid for Scientific Research (C)
• 财政年份: 2001
• 资助国家: 日本
• 起止时间: 2001 至 2002
• 项目状态: 已结题
• 来源: https://kaken.nii.ac.jp/grant/KAKENHI-PROJECT-13660088/
• 关键词: salt; ion transport system; Arabidopsis thaliana; HKTl; transporter; channel; K^+; Na^+; AtHKT1; K^+チャネル; イオン選択性; 膜貫通; H^+ antiporter; 小胞体膜

1. AtHKTl from Arabidopsis (AtHKTl) was found to form 4-fold membrane-pore-membrane structure.2. It is found that the P-loop of HKT transporters show identity only in one of glycine residues that mediates K^+ selectivity. HKT transporters share a common ancestor transporter with 4-loops.3. KATl shares typical similarity with other animal and plant K^+ channels. The voltage-sensing segments of S3 and S4 in KATl are posttranslationally integrated into the membrane only when specific interation occurs between them. The insertion process is a newly recognized second type of the membrane protein integration process.4. The aspartate in the transmembrane of Na^+/H^+ antiporter from a bacteria involves in H^+ permeation but not Na^+ permeation.5. The AtHKTl was expressed in vascular tissue in plant.6. AtHKTl plays a role in the recirculation of Na^+ in plant body.7. The K^+ permeation of HKT-type transporter in Synechocystis PCC6803 was measured. K^+ transport activity was activated by Na^+ using E. coli expression system.

1.拟南芥AtHKTl（AtHKTl）具有4倍膜-孔-膜结构.结果表明，HKT转运蛋白的P环只有一个甘氨酸残基具有相同性，这一氨基酸残基介导了K^+的选择性。HKT转运蛋白与4-环转运蛋白有共同的祖先。KAT 1与其他动物和植物K^+通道具有典型的相似性。KAT 1中的S3和S4的电压敏感区段仅当它们之间发生特异性相互作用时才被后序整合到膜中。插入过程是新近认识到的第二类膜蛋白整合过程.细菌Na^+/H^+逆向转运蛋白跨膜中的天冬氨酸参与H^+的渗透，但不参与Na^+的渗透。AtHKTl在植物维管组织中表达. AtHKTl在植物体内Na^+的再循环中起作用。测定了集胞藻6803中HKT型转运蛋白的K^+渗透能力。利用E. coli表达系统。

项目成果

Kato,Y., Sakaguchi,M., Mori Y., Saito,K., Nakamura,T., Bakker,E.P., Sato,Y., Goshima,S. and Uozumi,N.: "Evidence in support of a four transmembrane-pore-transmembrane topology model for the Arabidopsis thaliana Na^+/K^+ translocating AtHKTl protein, a mem

加藤，Y.，坂口，M.，森 Y.，斋藤，K.，中村，T.，巴克，E.P.，佐藤，Y.，五岛，S。

魚住 信之: "化学と生物(植物のK^+チャネル・K^+トランスポーターはどこまでわかったか)"5 (2001)

鱼住伸行：“化学与生物学（我们对植物中的 K^+ 通道和 K^+ 转运蛋白了解多少）”5 (2001)

Sato,Y., Sakaguchi,M., Goshima,S., Nakamura,T., and Uozumi,N.: "Integration of Shaker-type K^+ channel, KATl into the endoplasmic reticulum membrane : Synergistic insertion of voltage sensing segments, S3-S4 and independent insertion of pore-forming segme

Sato,Y.、Sakaguchi,M.、Goshima,S.、Nakamura,T. 和 Uozumi,N.：“将 Shaker 型 K^ 通道、KAT1 整合到内质网膜中：电压传感段的协同插入，

Master, P., et al.: "Altered shoot/root Na^+ distribution and bifurcating salt sensitivity in Arabidopsis by genetic disruption of the Na^+ transporter AtHKT1"FEBS Letters. 531. 157-161 (2002)

Master, P. 等人：“通过 Na+ 转运蛋白 AtHKT1 的遗传破坏改变了拟南芥中的芽/根 Na+ 分布和分叉盐敏感性”FEBS Letters。

Sato,Y., Hosoo,Y., Sakaguchi,M., and Uozumi,N.: "(2003) Requirement of negative residues, Asp 95 and Asp 105, in S2 on channel function and membrane integration of voltage-dependent K^+ channel, KATl"Biosci.Biotech.Biochem.. 67. 923-926 (2003)

Sato,Y.、Hosoo,Y.、Sakaguchi,M. 和 Uozumi,N.：“(2003) S2 中负残基 Asp 95 和 Asp 105 对电压依赖性 K^ 的通道功能和膜整合的要求