| Project/Area Number |
13660088
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
応用微生物学・応用生物化学
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| Research Institution | NAGOYA UNIVERSITY |
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Principal Investigator |
UOZUMI Nobuyuki Nagoya University, Bioscience Center Associate Professor, 生物分子応答研究センター, 助教授 (40223515)
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| Project Period (FY) |
2001 – 2002
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| Project Status |
Completed (Fiscal Year 2002)
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| Budget Amount *help |
¥3,600,000 (Direct Cost: ¥3,600,000)
Fiscal Year 2002: ¥1,600,000 (Direct Cost: ¥1,600,000)
Fiscal Year 2001: ¥2,000,000 (Direct Cost: ¥2,000,000)
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| Keywords | 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 |
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| Research Abstract |
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.
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